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Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12
The reversible formation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-CP12-phosphoribulokinase (PRK) supramolecular complex, identified in oxygenic photosynthetic organisms, provides light-dependent Calvin cycle regulation in a coordinated manner. An intrinsically disordered protein (IDP) C...
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| Published in: | Structure (London) 2011-12, Vol.19 (12), p.1846-1854 |
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| container_end_page | 1854 |
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| creator | Matsumura, Hiroyoshi Kai, Akihiro Maeda, Takayuki Tamoi, Masahiro Satoh, Atsuko Tamura, Haruka Hirose, Mika Ogawa, Taketo Kizu, Natsuko Wadano, Akira Inoue, Tsuyoshi Shigeoka, Shigeru |
| description | The reversible formation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-CP12-phosphoribulokinase (PRK) supramolecular complex, identified in oxygenic photosynthetic organisms, provides light-dependent Calvin cycle regulation in a coordinated manner. An intrinsically disordered protein (IDP) CP12 acts as a linker to sequentially bind GAPDH and PRK to downregulate both enzymes. Here, we report the crystal structures of the ternary GAPDH-CP12-NAD and binary GAPDH-NAD complexes from Synechococcus elongates. The GAPDH-CP12 complex structure reveals that the oxidized CP12 becomes partially structured upon GAPDH binding. The C-terminus of CP12 is inserted into the active-site region of GAPDH, resulting in competitive inhibition of GAPDH. This study also provides insight into how the GAPDH-CP12 complex is dissociated by a high NADP(H)/NAD(H) ratio. An unexpected increase in negative charge potential that emerged upon CP12 binding highlights the biological function of CP12 in the sequential assembly of the supramolecular complex.
► The C-terminal region of CP12 is bound to GAPDH in complex with NAD ► The CP12 covers the substrate binding site of GAPDH ► NAD stabilizes the GAPDH-CP12 complex, but NADP does not ► An unexpected increase in negative charge potential emerges upon CP12 binding. |
| doi_str_mv | 10.1016/j.str.2011.08.016 |
| format | article |
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► The C-terminal region of CP12 is bound to GAPDH in complex with NAD ► The CP12 covers the substrate binding site of GAPDH ► NAD stabilizes the GAPDH-CP12 complex, but NADP does not ► An unexpected increase in negative charge potential emerges upon CP12 binding.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - metabolism</subject><subject>Binding Sites</subject><subject>Crystallography, X-Ray</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry</subject><subject>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Multiprotein Complexes - chemistry</subject><subject>Multiprotein Complexes - metabolism</subject><subject>NAD - chemistry</subject><subject>NAD - metabolism</subject><subject>Synechococcus - enzymology</subject><subject>Synechococcus - metabolism</subject><issn>0969-2126</issn><issn>1878-4186</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</creationdate><recordtype>article</recordtype><recordid>eNp9kM1u1DAUhS0EokPhAdgg71gl9XXiOBarMoVSqRIjftaWY990PMrEg-2MlAfgvckwLUtWVzr6zifdQ8hbYCUwaK52Zcqx5AygZG25JM_IClrZFjW0zXOyYqpRBQfeXJBXKe0YY1ww9pJccA6iEkyuyO_vOU42TxHpR5N8on2ING-RfsOHaTDZh5GGnt4Os8VoBofb2WFRFZttSIetyUhvTlEMDziahPTaZn_0eaZHb_567sYc_Zi8NcMw0xufQnQY0dFNDBn9SNcb4K_Ji94MCd883kvy8_OnH-svxf3X27v19X1h6wZyoXgPpgJphauFEaYB13e96mRf1wxQyrZrlTAoRaMkB9tVTdtYIw1X0nJ01SV5f_YeYvg1Ycp675PFYTAjhilpBaBqXldiIeFM2hhSitjrQ_R7E2cNTJ_G1zu9jK9P42vW6iVZOu8e7VO3R_ev8bT2Anw4A7j8ePQYdbIeR4vOR7RZu-D_o_8DAs-W6w</recordid><startdate>20111207</startdate><enddate>20111207</enddate><creator>Matsumura, Hiroyoshi</creator><creator>Kai, Akihiro</creator><creator>Maeda, Takayuki</creator><creator>Tamoi, Masahiro</creator><creator>Satoh, Atsuko</creator><creator>Tamura, Haruka</creator><creator>Hirose, Mika</creator><creator>Ogawa, Taketo</creator><creator>Kizu, Natsuko</creator><creator>Wadano, Akira</creator><creator>Inoue, Tsuyoshi</creator><creator>Shigeoka, Shigeru</creator><general>Elsevier Inc</general><scope>6I.</scope><scope>AAFTH</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>20111207</creationdate><title>Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12</title><author>Matsumura, Hiroyoshi ; Kai, Akihiro ; Maeda, Takayuki ; Tamoi, Masahiro ; Satoh, Atsuko ; Tamura, Haruka ; Hirose, Mika ; Ogawa, Taketo ; Kizu, Natsuko ; Wadano, Akira ; Inoue, Tsuyoshi ; Shigeoka, Shigeru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c461t-92f1a317c5d45a5a61dfbf9b7f4401e778b895ae7569721cb3686ca7a297c2ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - chemistry</topic><topic>Bacterial Proteins - metabolism</topic><topic>Binding Sites</topic><topic>Crystallography, X-Ray</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry</topic><topic>Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Multiprotein Complexes - chemistry</topic><topic>Multiprotein Complexes - metabolism</topic><topic>NAD - chemistry</topic><topic>NAD - metabolism</topic><topic>Synechococcus - enzymology</topic><topic>Synechococcus - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Matsumura, Hiroyoshi</creatorcontrib><creatorcontrib>Kai, Akihiro</creatorcontrib><creatorcontrib>Maeda, Takayuki</creatorcontrib><creatorcontrib>Tamoi, Masahiro</creatorcontrib><creatorcontrib>Satoh, Atsuko</creatorcontrib><creatorcontrib>Tamura, Haruka</creatorcontrib><creatorcontrib>Hirose, Mika</creatorcontrib><creatorcontrib>Ogawa, Taketo</creatorcontrib><creatorcontrib>Kizu, Natsuko</creatorcontrib><creatorcontrib>Wadano, Akira</creatorcontrib><creatorcontrib>Inoue, Tsuyoshi</creatorcontrib><creatorcontrib>Shigeoka, Shigeru</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</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>Structure (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Matsumura, Hiroyoshi</au><au>Kai, Akihiro</au><au>Maeda, Takayuki</au><au>Tamoi, Masahiro</au><au>Satoh, Atsuko</au><au>Tamura, Haruka</au><au>Hirose, Mika</au><au>Ogawa, Taketo</au><au>Kizu, Natsuko</au><au>Wadano, Akira</au><au>Inoue, Tsuyoshi</au><au>Shigeoka, Shigeru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12</atitle><jtitle>Structure (London)</jtitle><addtitle>Structure</addtitle><date>2011-12-07</date><risdate>2011</risdate><volume>19</volume><issue>12</issue><spage>1846</spage><epage>1854</epage><pages>1846-1854</pages><issn>0969-2126</issn><eissn>1878-4186</eissn><notes>ObjectType-Article-1</notes><notes>SourceType-Scholarly Journals-1</notes><notes>ObjectType-Feature-2</notes><notes>content type line 23</notes><abstract>The reversible formation of a glyceraldehyde-3-phosphate dehydrogenase (GAPDH)-CP12-phosphoribulokinase (PRK) supramolecular complex, identified in oxygenic photosynthetic organisms, provides light-dependent Calvin cycle regulation in a coordinated manner. An intrinsically disordered protein (IDP) CP12 acts as a linker to sequentially bind GAPDH and PRK to downregulate both enzymes. Here, we report the crystal structures of the ternary GAPDH-CP12-NAD and binary GAPDH-NAD complexes from Synechococcus elongates. The GAPDH-CP12 complex structure reveals that the oxidized CP12 becomes partially structured upon GAPDH binding. The C-terminus of CP12 is inserted into the active-site region of GAPDH, resulting in competitive inhibition of GAPDH. This study also provides insight into how the GAPDH-CP12 complex is dissociated by a high NADP(H)/NAD(H) ratio. An unexpected increase in negative charge potential that emerged upon CP12 binding highlights the biological function of CP12 in the sequential assembly of the supramolecular complex.
► The C-terminal region of CP12 is bound to GAPDH in complex with NAD ► The CP12 covers the substrate binding site of GAPDH ► NAD stabilizes the GAPDH-CP12 complex, but NADP does not ► An unexpected increase in negative charge potential emerges upon CP12 binding.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>22153507</pmid><doi>10.1016/j.str.2011.08.016</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Structure (London), 2011-12, Vol.19 (12), p.1846-1854 |
| issn | 0969-2126 1878-4186 |
| language | eng |
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| source | BACON - Elsevier - GLOBAL_SCIENCEDIRECT-OPENACCESS |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - metabolism Binding Sites Crystallography, X-Ray Glyceraldehyde-3-Phosphate Dehydrogenases - chemistry Glyceraldehyde-3-Phosphate Dehydrogenases - metabolism Molecular Sequence Data Multiprotein Complexes - chemistry Multiprotein Complexes - metabolism NAD - chemistry NAD - metabolism Synechococcus - enzymology Synechococcus - metabolism |
| title | Structure Basis for the Regulation of Glyceraldehyde-3-Phosphate Dehydrogenase Activity via the Intrinsically Disordered Protein CP12 |
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