Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris

A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structur...

Full description

Saved in:
Bibliographic Details
Published in:Biochemistry (Easton) 2001-01, Vol.40 (2), p.569-576
Main Authors: Mattei, Benedetta, Bernalda, Maria Scala, Federici, Luca, Roepstorff, Peter, Cervone, Felice, Boffi, Alberto
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Circular Dichroism
Disulfides - chemistry
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - metabolism
Fabaceae
Glycosylation
Leucine - metabolism
Molecular Sequence Data
Plant Proteins - chemistry
Plant Proteins - metabolism
Plants, Medicinal
Polygalacturonase - antagonists & inhibitors
Protein Processing, Post-Translational
Protein Structure, Secondary
Repetitive Sequences, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectroscopy, Fourier Transform Infrared
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
cited_by cdi_FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43
cites cdi_FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43
container_end_page 576
container_issue 2
container_start_page 569
container_title Biochemistry (Easton)
container_volume 40
creator Mattei, Benedetta
Bernalda, Maria Scala
Federici, Luca
Roepstorff, Peter
Cervone, Felice
Boffi, Alberto
description A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structure prediction methods indicated the presence of 12 α- and 12 β-segments, thus allowing a schematic representation of three domains of the protein, namely, the central LRR region and the two cysteine-rich flanking domains. Peptides from endoproteinase-degraded PGIP were analyzed by mass spectrometry, and four disulfide bonds were identified. Mass spectrometric analysis in combination with glycosidase treatments revealed two N-linked oligosaccharides located on Asn 64 and Asn 141. The main structure resembled the typical complex plant N-glycan consisting of a core pentasaccharide β1,2-xylosylated, carrying an α1,3-fucose linked to the innermost N-acetylglucosamine and one outer arm N-acetylglucosamine residue. The schematic representation of PGIP structural domains is discussed in the framework of the structure and function of LRR proteins.
doi_str_mv 10.1021/bi0017632
format article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_70575487</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>70575487</sourcerecordid><originalsourceid>FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43</originalsourceid><addsrcrecordid>eNptkc1uEzEUhS0EoqGw4AWQNyC6cLFnPOPMElU0BKVilAQhsbE8njuJy8QO_kH0aXjVuk1aNqzuvTqfzpXOQeg1o-eMFuxDZyhloi6LJ2jCqoIS3jTVUzShlNakaGp6gl6EcJ1PTgV_jk4YY3xKq2KC_q5AO9srf4NX0ScdkwesbI9bFyJZe2XDqKJxVo34yvVmMPr-DNgNOG4BLyBpY4Esjd7iJexBRdx6F8FY3M7mLX7fuvFmo0Z15519ApC53ZrORGM3D-gZHrzb4XabZTemgH-ncaO8CS_Rs0GNAV4d5yn6dvlpffGZLL7O5hcfF0SVvImkFlUtOGcMptDwvgNWlJVSUAqm675uhOj6nA_PCxNTIQpeNkINvehpobni5Sl6d_Dde_crQYhyZ4KGcVQWXApS0EpUfCoyeHYAtXcheBjk3ptdzk8yKu_akI9tZPbN0TR1O-j_kcf4M0AOgAkR_jzqyv-UtShFJdftSi75jy_fZ5dXssr82wOvdJDXLvlcS_jP41u4z6F7</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>70575487</pqid></control><display><type>article</type><title>Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris</title><source>American Chemical Society:Jisc Collections:American Chemical Society Read &amp; Publish Agreement 2022-2024 (Reading list)</source><creator>Mattei, Benedetta ; Bernalda, Maria Scala ; Federici, Luca ; Roepstorff, Peter ; Cervone, Felice ; Boffi, Alberto</creator><creatorcontrib>Mattei, Benedetta ; Bernalda, Maria Scala ; Federici, Luca ; Roepstorff, Peter ; Cervone, Felice ; Boffi, Alberto</creatorcontrib><description>A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structure prediction methods indicated the presence of 12 α- and 12 β-segments, thus allowing a schematic representation of three domains of the protein, namely, the central LRR region and the two cysteine-rich flanking domains. Peptides from endoproteinase-degraded PGIP were analyzed by mass spectrometry, and four disulfide bonds were identified. Mass spectrometric analysis in combination with glycosidase treatments revealed two N-linked oligosaccharides located on Asn 64 and Asn 141. The main structure resembled the typical complex plant N-glycan consisting of a core pentasaccharide β1,2-xylosylated, carrying an α1,3-fucose linked to the innermost N-acetylglucosamine and one outer arm N-acetylglucosamine residue. The schematic representation of PGIP structural domains is discussed in the framework of the structure and function of LRR proteins.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi0017632</identifier><identifier>PMID: 11148052</identifier><language>eng</language><publisher>United States: American Chemical Society</publisher><subject>Amino Acid Sequence ; Circular Dichroism ; Disulfides - chemistry ; Enzyme Inhibitors - chemistry ; Enzyme Inhibitors - metabolism ; Fabaceae ; Glycosylation ; Leucine - metabolism ; Molecular Sequence Data ; Plant Proteins - chemistry ; Plant Proteins - metabolism ; Plants, Medicinal ; Polygalacturonase - antagonists &amp; inhibitors ; Protein Processing, Post-Translational ; Protein Structure, Secondary ; Repetitive Sequences, Amino Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Spectroscopy, Fourier Transform Infrared</subject><ispartof>Biochemistry (Easton), 2001-01, Vol.40 (2), p.569-576</ispartof><rights>Copyright © 2001 American Chemical Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43</citedby><cites>FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>315,783,787,27936,27937</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11148052$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mattei, Benedetta</creatorcontrib><creatorcontrib>Bernalda, Maria Scala</creatorcontrib><creatorcontrib>Federici, Luca</creatorcontrib><creatorcontrib>Roepstorff, Peter</creatorcontrib><creatorcontrib>Cervone, Felice</creatorcontrib><creatorcontrib>Boffi, Alberto</creatorcontrib><title>Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structure prediction methods indicated the presence of 12 α- and 12 β-segments, thus allowing a schematic representation of three domains of the protein, namely, the central LRR region and the two cysteine-rich flanking domains. Peptides from endoproteinase-degraded PGIP were analyzed by mass spectrometry, and four disulfide bonds were identified. Mass spectrometric analysis in combination with glycosidase treatments revealed two N-linked oligosaccharides located on Asn 64 and Asn 141. The main structure resembled the typical complex plant N-glycan consisting of a core pentasaccharide β1,2-xylosylated, carrying an α1,3-fucose linked to the innermost N-acetylglucosamine and one outer arm N-acetylglucosamine residue. The schematic representation of PGIP structural domains is discussed in the framework of the structure and function of LRR proteins.</description><subject>Amino Acid Sequence</subject><subject>Circular Dichroism</subject><subject>Disulfides - chemistry</subject><subject>Enzyme Inhibitors - chemistry</subject><subject>Enzyme Inhibitors - metabolism</subject><subject>Fabaceae</subject><subject>Glycosylation</subject><subject>Leucine - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Plant Proteins - chemistry</subject><subject>Plant Proteins - metabolism</subject><subject>Plants, Medicinal</subject><subject>Polygalacturonase - antagonists &amp; inhibitors</subject><subject>Protein Processing, Post-Translational</subject><subject>Protein Structure, Secondary</subject><subject>Repetitive Sequences, Amino Acid</subject><subject>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</subject><subject>Spectroscopy, Fourier Transform Infrared</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><recordid>eNptkc1uEzEUhS0EoqGw4AWQNyC6cLFnPOPMElU0BKVilAQhsbE8njuJy8QO_kH0aXjVuk1aNqzuvTqfzpXOQeg1o-eMFuxDZyhloi6LJ2jCqoIS3jTVUzShlNakaGp6gl6EcJ1PTgV_jk4YY3xKq2KC_q5AO9srf4NX0ScdkwesbI9bFyJZe2XDqKJxVo34yvVmMPr-DNgNOG4BLyBpY4Esjd7iJexBRdx6F8FY3M7mLX7fuvFmo0Z15519ApC53ZrORGM3D-gZHrzb4XabZTemgH-ncaO8CS_Rs0GNAV4d5yn6dvlpffGZLL7O5hcfF0SVvImkFlUtOGcMptDwvgNWlJVSUAqm675uhOj6nA_PCxNTIQpeNkINvehpobni5Sl6d_Dde_crQYhyZ4KGcVQWXApS0EpUfCoyeHYAtXcheBjk3ptdzk8yKu_akI9tZPbN0TR1O-j_kcf4M0AOgAkR_jzqyv-UtShFJdftSi75jy_fZ5dXssr82wOvdJDXLvlcS_jP41u4z6F7</recordid><startdate>20010116</startdate><enddate>20010116</enddate><creator>Mattei, Benedetta</creator><creator>Bernalda, Maria Scala</creator><creator>Federici, Luca</creator><creator>Roepstorff, Peter</creator><creator>Cervone, Felice</creator><creator>Boffi, Alberto</creator><general>American Chemical Society</general><scope>BSCLL</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20010116</creationdate><title>Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris</title><author>Mattei, Benedetta ; Bernalda, Maria Scala ; Federici, Luca ; Roepstorff, Peter ; Cervone, Felice ; Boffi, Alberto</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Circular Dichroism</topic><topic>Disulfides - chemistry</topic><topic>Enzyme Inhibitors - chemistry</topic><topic>Enzyme Inhibitors - metabolism</topic><topic>Fabaceae</topic><topic>Glycosylation</topic><topic>Leucine - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Plant Proteins - chemistry</topic><topic>Plant Proteins - metabolism</topic><topic>Plants, Medicinal</topic><topic>Polygalacturonase - antagonists &amp; inhibitors</topic><topic>Protein Processing, Post-Translational</topic><topic>Protein Structure, Secondary</topic><topic>Repetitive Sequences, Amino Acid</topic><topic>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</topic><topic>Spectroscopy, Fourier Transform Infrared</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mattei, Benedetta</creatorcontrib><creatorcontrib>Bernalda, Maria Scala</creatorcontrib><creatorcontrib>Federici, Luca</creatorcontrib><creatorcontrib>Roepstorff, Peter</creatorcontrib><creatorcontrib>Cervone, Felice</creatorcontrib><creatorcontrib>Boffi, Alberto</creatorcontrib><collection>Istex</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mattei, Benedetta</au><au>Bernalda, Maria Scala</au><au>Federici, Luca</au><au>Roepstorff, Peter</au><au>Cervone, Felice</au><au>Boffi, Alberto</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris</atitle><jtitle>Biochemistry (Easton)</jtitle><addtitle>Biochemistry</addtitle><date>2001-01-16</date><risdate>2001</risdate><volume>40</volume><issue>2</issue><spage>569</spage><epage>576</epage><pages>569-576</pages><issn>0006-2960</issn><eissn>1520-4995</eissn><abstract>A detailed analysis of the secondary structure has been carried out on the polygalacturonase-inhibiting protein (PGIP) from Phaseolus vulgaris, a leucine-rich repeat (LRR) protein present in the cell wall of many plants. Far-UV CD and infrared spectroscopies coupled to constrained secondary structure prediction methods indicated the presence of 12 α- and 12 β-segments, thus allowing a schematic representation of three domains of the protein, namely, the central LRR region and the two cysteine-rich flanking domains. Peptides from endoproteinase-degraded PGIP were analyzed by mass spectrometry, and four disulfide bonds were identified. Mass spectrometric analysis in combination with glycosidase treatments revealed two N-linked oligosaccharides located on Asn 64 and Asn 141. The main structure resembled the typical complex plant N-glycan consisting of a core pentasaccharide β1,2-xylosylated, carrying an α1,3-fucose linked to the innermost N-acetylglucosamine and one outer arm N-acetylglucosamine residue. The schematic representation of PGIP structural domains is discussed in the framework of the structure and function of LRR proteins.</abstract><cop>United States</cop><pub>American Chemical Society</pub><pmid>11148052</pmid><doi>10.1021/bi0017632</doi><tpages>8</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0006-2960
ispartof Biochemistry (Easton), 2001-01, Vol.40 (2), p.569-576
issn 0006-2960
1520-4995
language eng
recordid cdi_proquest_miscellaneous_70575487
source American Chemical Society:Jisc Collections:American Chemical Society Read & Publish Agreement 2022-2024 (Reading list)
subjects Amino Acid Sequence
Circular Dichroism
Disulfides - chemistry
Enzyme Inhibitors - chemistry
Enzyme Inhibitors - metabolism
Fabaceae
Glycosylation
Leucine - metabolism
Molecular Sequence Data
Plant Proteins - chemistry
Plant Proteins - metabolism
Plants, Medicinal
Polygalacturonase - antagonists & inhibitors
Protein Processing, Post-Translational
Protein Structure, Secondary
Repetitive Sequences, Amino Acid
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Spectroscopy, Fourier Transform Infrared
title Secondary Structure and Post-Translational Modifications of the Leucine-Rich Repeat Protein PGIP (Polygalacturonase-Inhibiting Protein) from Phaseolus vulgaris
url http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2024-11-13T17%3A16%3A42IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Secondary%20Structure%20and%20Post-Translational%20Modifications%20of%20the%20Leucine-Rich%20Repeat%20Protein%20PGIP%20(Polygalacturonase-Inhibiting%20Protein)%20from%20Phaseolus%20vulgaris&rft.jtitle=Biochemistry%20(Easton)&rft.au=Mattei,%20Benedetta&rft.date=2001-01-16&rft.volume=40&rft.issue=2&rft.spage=569&rft.epage=576&rft.pages=569-576&rft.issn=0006-2960&rft.eissn=1520-4995&rft_id=info:doi/10.1021/bi0017632&rft_dat=%3Cproquest_cross%3E70575487%3C/proquest_cross%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-a349t-675674411e8e94dbe1235aae371c6d6977bd63249771787724397afd7d02c4a43%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=70575487&rft_id=info:pmid/11148052&rfr_iscdi=true