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Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein
Abstract Anaeromyxobacter dehalogenans is a δ‐proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal‐reducing capabilities. To gain an understanding on A. dehalogenans' abilities to adapt to diverse environments we a...
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| Published in: | MicrobiologyOpen (Weinheim) 2013-10, Vol.2 (5), p.766-777 |
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| creator | Pokkuluri, P. Raj Dwulit‐Smith, Jeff Duke, Norma E. Wilton, Rosemarie Mack, Jamey C. Bearden, Jessica Rakowski, Ella Babnigg, Gyorgy Szurmant, Hendrik Joachimiak, Andrzej Schiffer, Marianne |
| description | Abstract
Anaeromyxobacter dehalogenans
is a δ‐proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal‐reducing capabilities. To gain an understanding on
A. dehalogenans'
abilities to adapt to diverse environments we analyzed its signal transduction proteins. The
A. dehalogenans
genome codes for a large number of sensor histidine kinases (
HK
) and methyl‐accepting chemotaxis proteins (
MCP
); among these 23
HK
and 11
MCP
proteins have a sensor domain in the periplasm. These proteins most likely contribute to adaptation to the organism's surroundings. We predicted their three‐dimensional folds and determined the structures of two of the periplasmic sensor domains by X‐ray diffraction. Most of the domains are predicted to have either
PAS
‐like or helical bundle structures, with two predicted to have solute‐binding protein fold, and another predicted to have a 6‐phosphogluconolactonase like fold. Atomic structures of two sensor domains confirmed the respective fold predictions. The Adeh_2942 sensor (
HK
) was found to have a helical bundle structure, and the Adeh_3718 sensor (
MCP
) has a
PAS
‐like structure. Interestingly, the Adeh_3718 sensor has an acetate moiety bound in a binding site typical for
PAS
‐like domains. Future work is needed to determine whether Adeh_3718 is involved in acetate sensing by
A. dehalogenans
. |
| doi_str_mv | 10.1002/mbo3.112 |
| format | article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_1634844</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>2290823822</sourcerecordid><originalsourceid>FETCH-LOGICAL-c1272-370099c45af9a557e9c6dc3ef37fb6d2400b466c956968e25255359be026244a3</originalsourceid><addsrcrecordid>eNpVkd1KAzEQhRdRsKjgIwS98aaanST7450U_6CgoF6HbHbWTe0mNUmhvfMRfBVfyScxpV7owDAD83E4zMmy45ye55TCxdA4dp7nsJONgHIxriood__s-9lRCDOaqqRQ8HyUfV1ZNV8HE4jryAK9WcxVGIwmAW1wnrRuUMYG0nk3kMRimuuVa5SOmK7Yq7l7RasSAmTySL4_PieX5Cn6pY5LjxtVZ_G_2lZMkd6EaFqTzm_GqoBE2Ta1i32S_mV0j4OLapUMLryLaOxhttepecCj33mQvdxcP0_uxtOH2_vJ1XSscyhhzEpK61pzobpaCVFirYtWM-xY2TVFC5zShheFrkVRFxWCACGYqBtMjwHOFTvITra6LrmUQZuIutfOWtRR5gXjFecJOt1Cydz7EkOUM7f06aVBAtS0AlYBJOpsS2nvQvDYyYU3g_JrmVO5CU5ugpMpOPYDekmNYg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>2290823822</pqid></control><display><type>article</type><title>Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein</title><source>Open Access: Wiley-Blackwell Open Access Journals</source><source>ProQuest - Publicly Available Content Database</source><source>PubMed Central</source><creator>Pokkuluri, P. Raj ; Dwulit‐Smith, Jeff ; Duke, Norma E. ; Wilton, Rosemarie ; Mack, Jamey C. ; Bearden, Jessica ; Rakowski, Ella ; Babnigg, Gyorgy ; Szurmant, Hendrik ; Joachimiak, Andrzej ; Schiffer, Marianne</creator><creatorcontrib>Pokkuluri, P. Raj ; Dwulit‐Smith, Jeff ; Duke, Norma E. ; Wilton, Rosemarie ; Mack, Jamey C. ; Bearden, Jessica ; Rakowski, Ella ; Babnigg, Gyorgy ; Szurmant, Hendrik ; Joachimiak, Andrzej ; Schiffer, Marianne</creatorcontrib><description>Abstract
Anaeromyxobacter dehalogenans
is a δ‐proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal‐reducing capabilities. To gain an understanding on
A. dehalogenans'
abilities to adapt to diverse environments we analyzed its signal transduction proteins. The
A. dehalogenans
genome codes for a large number of sensor histidine kinases (
HK
) and methyl‐accepting chemotaxis proteins (
MCP
); among these 23
HK
and 11
MCP
proteins have a sensor domain in the periplasm. These proteins most likely contribute to adaptation to the organism's surroundings. We predicted their three‐dimensional folds and determined the structures of two of the periplasmic sensor domains by X‐ray diffraction. Most of the domains are predicted to have either
PAS
‐like or helical bundle structures, with two predicted to have solute‐binding protein fold, and another predicted to have a 6‐phosphogluconolactonase like fold. Atomic structures of two sensor domains confirmed the respective fold predictions. The Adeh_2942 sensor (
HK
) was found to have a helical bundle structure, and the Adeh_3718 sensor (
MCP
) has a
PAS
‐like structure. Interestingly, the Adeh_3718 sensor has an acetate moiety bound in a binding site typical for
PAS
‐like domains. Future work is needed to determine whether Adeh_3718 is involved in acetate sensing by
A. dehalogenans
.</description><identifier>ISSN: 2045-8827</identifier><identifier>EISSN: 2045-8827</identifier><identifier>DOI: 10.1002/mbo3.112</identifier><language>eng</language><publisher>Bognor Regis: John Wiley & Sons, Inc</publisher><subject>Acetic acid ; Anaeromyxobacter ; Binding sites ; Bioremediation ; Chemotaxis ; Cloning ; Dechlorination ; Deoxyribonucleic acid ; DNA ; DNA polymerase ; Genomes ; Histidine ; Histidine kinase ; Kinases ; Motility ; Periplasm ; Predictions ; Protein folding ; Proteins ; Sediments ; Sensors ; Signal transduction ; Transcription factors</subject><ispartof>MicrobiologyOpen (Weinheim), 2013-10, Vol.2 (5), p.766-777</ispartof><rights>2013. This work is published under http://creativecommons.org/licenses/by/3.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c1272-370099c45af9a557e9c6dc3ef37fb6d2400b466c956968e25255359be026244a3</citedby><cites>FETCH-LOGICAL-c1272-370099c45af9a557e9c6dc3ef37fb6d2400b466c956968e25255359be026244a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.proquest.com/docview/2290823822/fulltextPDF?pq-origsite=primo$$EPDF$$P50$$Gproquest$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2290823822?pq-origsite=primo$$EHTML$$P50$$Gproquest$$Hfree_for_read</linktohtml><link.rule.ids>230,315,786,790,891,25783,27957,27958,37047,44625,75483</link.rule.ids><backlink>$$Uhttps://www.osti.gov/biblio/1634844$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Pokkuluri, P. Raj</creatorcontrib><creatorcontrib>Dwulit‐Smith, Jeff</creatorcontrib><creatorcontrib>Duke, Norma E.</creatorcontrib><creatorcontrib>Wilton, Rosemarie</creatorcontrib><creatorcontrib>Mack, Jamey C.</creatorcontrib><creatorcontrib>Bearden, Jessica</creatorcontrib><creatorcontrib>Rakowski, Ella</creatorcontrib><creatorcontrib>Babnigg, Gyorgy</creatorcontrib><creatorcontrib>Szurmant, Hendrik</creatorcontrib><creatorcontrib>Joachimiak, Andrzej</creatorcontrib><creatorcontrib>Schiffer, Marianne</creatorcontrib><title>Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein</title><title>MicrobiologyOpen (Weinheim)</title><description>Abstract
Anaeromyxobacter dehalogenans
is a δ‐proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal‐reducing capabilities. To gain an understanding on
A. dehalogenans'
abilities to adapt to diverse environments we analyzed its signal transduction proteins. The
A. dehalogenans
genome codes for a large number of sensor histidine kinases (
HK
) and methyl‐accepting chemotaxis proteins (
MCP
); among these 23
HK
and 11
MCP
proteins have a sensor domain in the periplasm. These proteins most likely contribute to adaptation to the organism's surroundings. We predicted their three‐dimensional folds and determined the structures of two of the periplasmic sensor domains by X‐ray diffraction. Most of the domains are predicted to have either
PAS
‐like or helical bundle structures, with two predicted to have solute‐binding protein fold, and another predicted to have a 6‐phosphogluconolactonase like fold. Atomic structures of two sensor domains confirmed the respective fold predictions. The Adeh_2942 sensor (
HK
) was found to have a helical bundle structure, and the Adeh_3718 sensor (
MCP
) has a
PAS
‐like structure. Interestingly, the Adeh_3718 sensor has an acetate moiety bound in a binding site typical for
PAS
‐like domains. Future work is needed to determine whether Adeh_3718 is involved in acetate sensing by
A. dehalogenans
.</description><subject>Acetic acid</subject><subject>Anaeromyxobacter</subject><subject>Binding sites</subject><subject>Bioremediation</subject><subject>Chemotaxis</subject><subject>Cloning</subject><subject>Dechlorination</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>DNA polymerase</subject><subject>Genomes</subject><subject>Histidine</subject><subject>Histidine kinase</subject><subject>Kinases</subject><subject>Motility</subject><subject>Periplasm</subject><subject>Predictions</subject><subject>Protein folding</subject><subject>Proteins</subject><subject>Sediments</subject><subject>Sensors</subject><subject>Signal transduction</subject><subject>Transcription factors</subject><issn>2045-8827</issn><issn>2045-8827</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>PIMPY</sourceid><recordid>eNpVkd1KAzEQhRdRsKjgIwS98aaanST7450U_6CgoF6HbHbWTe0mNUmhvfMRfBVfyScxpV7owDAD83E4zMmy45ye55TCxdA4dp7nsJONgHIxriood__s-9lRCDOaqqRQ8HyUfV1ZNV8HE4jryAK9WcxVGIwmAW1wnrRuUMYG0nk3kMRimuuVa5SOmK7Yq7l7RasSAmTySL4_PieX5Cn6pY5LjxtVZ_G_2lZMkd6EaFqTzm_GqoBE2Ta1i32S_mV0j4OLapUMLryLaOxhttepecCj33mQvdxcP0_uxtOH2_vJ1XSscyhhzEpK61pzobpaCVFirYtWM-xY2TVFC5zShheFrkVRFxWCACGYqBtMjwHOFTvITra6LrmUQZuIutfOWtRR5gXjFecJOt1Cydz7EkOUM7f06aVBAtS0AlYBJOpsS2nvQvDYyYU3g_JrmVO5CU5ugpMpOPYDekmNYg</recordid><startdate>20131001</startdate><enddate>20131001</enddate><creator>Pokkuluri, P. Raj</creator><creator>Dwulit‐Smith, Jeff</creator><creator>Duke, Norma E.</creator><creator>Wilton, Rosemarie</creator><creator>Mack, Jamey C.</creator><creator>Bearden, Jessica</creator><creator>Rakowski, Ella</creator><creator>Babnigg, Gyorgy</creator><creator>Szurmant, Hendrik</creator><creator>Joachimiak, Andrzej</creator><creator>Schiffer, Marianne</creator><general>John Wiley & Sons, Inc</general><general>Wiley Blackwell (John Wiley & Sons)</general><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7X7</scope><scope>7XB</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>OTOTI</scope></search><sort><creationdate>20131001</creationdate><title>Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein</title><author>Pokkuluri, P. Raj ; Dwulit‐Smith, Jeff ; Duke, Norma E. ; Wilton, Rosemarie ; Mack, Jamey C. ; Bearden, Jessica ; Rakowski, Ella ; Babnigg, Gyorgy ; Szurmant, Hendrik ; Joachimiak, Andrzej ; Schiffer, Marianne</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c1272-370099c45af9a557e9c6dc3ef37fb6d2400b466c956968e25255359be026244a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Acetic acid</topic><topic>Anaeromyxobacter</topic><topic>Binding sites</topic><topic>Bioremediation</topic><topic>Chemotaxis</topic><topic>Cloning</topic><topic>Dechlorination</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>DNA polymerase</topic><topic>Genomes</topic><topic>Histidine</topic><topic>Histidine kinase</topic><topic>Kinases</topic><topic>Motility</topic><topic>Periplasm</topic><topic>Predictions</topic><topic>Protein folding</topic><topic>Proteins</topic><topic>Sediments</topic><topic>Sensors</topic><topic>Signal transduction</topic><topic>Transcription factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pokkuluri, P. Raj</creatorcontrib><creatorcontrib>Dwulit‐Smith, Jeff</creatorcontrib><creatorcontrib>Duke, Norma E.</creatorcontrib><creatorcontrib>Wilton, Rosemarie</creatorcontrib><creatorcontrib>Mack, Jamey C.</creatorcontrib><creatorcontrib>Bearden, Jessica</creatorcontrib><creatorcontrib>Rakowski, Ella</creatorcontrib><creatorcontrib>Babnigg, Gyorgy</creatorcontrib><creatorcontrib>Szurmant, Hendrik</creatorcontrib><creatorcontrib>Joachimiak, Andrzej</creatorcontrib><creatorcontrib>Schiffer, Marianne</creatorcontrib><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>ProQuest Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni)</collection><collection>ProQuest Central</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>AUTh Library subscriptions: ProQuest Central</collection><collection>ProQuest Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection (Proquest) (PQ_SDU_P3)</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biological Sciences</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest - Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>OSTI.GOV</collection><jtitle>MicrobiologyOpen (Weinheim)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pokkuluri, P. Raj</au><au>Dwulit‐Smith, Jeff</au><au>Duke, Norma E.</au><au>Wilton, Rosemarie</au><au>Mack, Jamey C.</au><au>Bearden, Jessica</au><au>Rakowski, Ella</au><au>Babnigg, Gyorgy</au><au>Szurmant, Hendrik</au><au>Joachimiak, Andrzej</au><au>Schiffer, Marianne</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein</atitle><jtitle>MicrobiologyOpen (Weinheim)</jtitle><date>2013-10-01</date><risdate>2013</risdate><volume>2</volume><issue>5</issue><spage>766</spage><epage>777</epage><pages>766-777</pages><issn>2045-8827</issn><eissn>2045-8827</eissn><notes>USDOE</notes><abstract>Abstract
Anaeromyxobacter dehalogenans
is a δ‐proteobacterium found in diverse soils and sediments. It is of interest in bioremediation efforts due to its dechlorination and metal‐reducing capabilities. To gain an understanding on
A. dehalogenans'
abilities to adapt to diverse environments we analyzed its signal transduction proteins. The
A. dehalogenans
genome codes for a large number of sensor histidine kinases (
HK
) and methyl‐accepting chemotaxis proteins (
MCP
); among these 23
HK
and 11
MCP
proteins have a sensor domain in the periplasm. These proteins most likely contribute to adaptation to the organism's surroundings. We predicted their three‐dimensional folds and determined the structures of two of the periplasmic sensor domains by X‐ray diffraction. Most of the domains are predicted to have either
PAS
‐like or helical bundle structures, with two predicted to have solute‐binding protein fold, and another predicted to have a 6‐phosphogluconolactonase like fold. Atomic structures of two sensor domains confirmed the respective fold predictions. The Adeh_2942 sensor (
HK
) was found to have a helical bundle structure, and the Adeh_3718 sensor (
MCP
) has a
PAS
‐like structure. Interestingly, the Adeh_3718 sensor has an acetate moiety bound in a binding site typical for
PAS
‐like domains. Future work is needed to determine whether Adeh_3718 is involved in acetate sensing by
A. dehalogenans
.</abstract><cop>Bognor Regis</cop><pub>John Wiley & Sons, Inc</pub><doi>10.1002/mbo3.112</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 2045-8827 |
| ispartof | MicrobiologyOpen (Weinheim), 2013-10, Vol.2 (5), p.766-777 |
| issn | 2045-8827 2045-8827 |
| language | eng |
| recordid | cdi_osti_scitechconnect_1634844 |
| source | Open Access: Wiley-Blackwell Open Access Journals; ProQuest - Publicly Available Content Database; PubMed Central |
| subjects | Acetic acid Anaeromyxobacter Binding sites Bioremediation Chemotaxis Cloning Dechlorination Deoxyribonucleic acid DNA DNA polymerase Genomes Histidine Histidine kinase Kinases Motility Periplasm Predictions Protein folding Proteins Sediments Sensors Signal transduction Transcription factors |
| title | Analysis of periplasmic sensor domains from Anaeromyxobacter dehalogenans 2 CP ‐C: Structure of one sensor domain from a histidine kinase and another from a chemotaxis protein |
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