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| | <StructureSection load='3rvd' size='340' side='right'caption='[[3rvd]], [[Resolution|resolution]] 2.70Å' scene=''> | | <StructureSection load='3rvd' size='340' side='right'caption='[[3rvd]], [[Resolution|resolution]] 2.70Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3rvd]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3rvd]] is a 16 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3RVD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3RVD FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[3k2b|3k2b]], [[3qv1|3qv1]]</div></td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">At3g26650, GAPA, MLJ15.4, MLJ15_5 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At3g26650 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), T12C14_110, At3g62410 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</td></tr> | + | |
| - | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+))_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.2.1.13 1.2.1.13] </span></td></tr>
| + | |
| | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvd OCA], [https://pdbe.org/3rvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvd RCSB], [https://www.ebi.ac.uk/pdbsum/3rvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvd ProSAT]</span></td></tr> | | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3rvd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3rvd OCA], [https://pdbe.org/3rvd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3rvd RCSB], [https://www.ebi.ac.uk/pdbsum/3rvd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3rvd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/G3PA1_ARATH G3PA1_ARATH]] Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity). [[https://www.uniprot.org/uniprot/CP122_ARATH CP122_ARATH]] Acts as a linker essential in the assembly of a core complex of PRK/GAPDH. Coordinates the reversible inactivation of chloroplast enzymes GAPDH and PRK during darkness in photosynthetic tissues.<ref>PMID:16258009</ref> <ref>PMID:20399532</ref>
| + | [https://www.uniprot.org/uniprot/G3PA1_ARATH G3PA1_ARATH] Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Arath]] | + | [[Category: Arabidopsis thaliana]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Falini, G]] | + | [[Category: Falini G]] |
| - | [[Category: Fermani, S]] | + | [[Category: Fermani S]] |
| - | [[Category: Marri, L]] | + | [[Category: Marri L]] |
| - | [[Category: Sparla, F]] | + | [[Category: Sparla F]] |
| - | [[Category: Thumiger, A]] | + | [[Category: Thumiger A]] |
| - | [[Category: Trost, P]] | + | [[Category: Trost P]] |
| - | [[Category: Binary complex]]
| + | |
| - | [[Category: Calvin cycle]]
| + | |
| - | [[Category: Chloroplast]]
| + | |
| - | [[Category: Oxidoreductase-protein binding complex]]
| + | |
| - | [[Category: Rossmann fold]]
| + | |
| Structural highlights
Function
G3PA1_ARATH Involved in the photosynthetic reductive pentose phosphate pathway (Calvin-Benson cycle). Catalyzes the reduction of 1,3-diphosphoglycerate by NADPH (By similarity).
Publication Abstract from PubMed
Carbon assimilation in plants is regulated by the reduction of specific protein disulfides by light and their re-oxidation in the dark. The redox switch CP12 is an intrinsically disordered protein that can form two disulfide bridges. In the dark oxidized CP12 forms an inactive supramolecular complex with glyceraldehyde-3-phosphate dehydrogenase (GAPDH) and phosphoribulokinase, two enzymes of the carbon assimilation cycle. Here we show that binding of CP12 to GAPDH, the first step of ternary complex formation, follows an integrated mechanism that combines conformational selection with induced folding steps. Initially, a CP12 conformation characterized by a circular structural motif including the C-terminal disulfide is selected by GAPDH. Subsequently, the induced folding of the flexible C-terminal tail of CP12 in the active site of GAPDH stabilizes the binary complex. Formation of several hydrogen bonds compensates the entropic cost of CP12 fixation and terminates the interaction mechanism that contributes to carbon assimilation control.
Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly.,Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P J Biol Chem. 2012 Jun 15;287(25):21372-83. Epub 2012 Apr 18. PMID:22514274[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fermani S, Trivelli X, Sparla F, Thumiger A, Calvaresi M, Marri L, Falini G, Zerbetto F, Trost P. Conformational Selection and Folding-upon-binding of Intrinsically Disordered Protein CP12 Regulate Photosynthetic Enzymes Assembly. J Biol Chem. 2012 Jun 15;287(25):21372-83. Epub 2012 Apr 18. PMID:22514274 doi:10.1074/jbc.M112.350355
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