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3qv1

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Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.

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 ==Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.==
-<StructureSection load='3qv1' size='340' side='right' caption='[[3qv1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
+<StructureSection load='3qv1' size='340' side='right'caption='[[3qv1]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3qv1]] is a 9 chain structure with sequence from [http://en.wikipedia.org/wiki/Arath Arath]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QV1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QV1 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3qv1]] is a 9 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=3QV1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3QV1 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3k2b|3k2b]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>, <scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</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 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH]), At3g62410, T12C14_110 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=3702 ARATH])</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=3qv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qv1 OCA], [https://pdbe.org/3qv1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3qv1 RCSB], [https://www.ebi.ac.uk/pdbsum/3qv1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3qv1 ProSAT]</span></td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Glyceraldehyde-3-phosphate_dehydrogenase_(NADP(+))_(phosphorylating) Glyceraldehyde-3-phosphate dehydrogenase (NADP(+)) (phosphorylating)], with EC number [http://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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3qv1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qv1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qv1 RCSB], [http://www.ebi.ac.uk/pdbsum/3qv1 PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://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). [[http://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;">
-== 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<ref>PMID:22514274</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+==See Also==
-</div>
+*[[Glyceraldehyde-3-phosphate dehydrogenase 3D structures|Glyceraldehyde-3-phosphate dehydrogenase 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Arath]]
+[[Category: Arabidopsis thaliana]]
-[[Category: Falini, G]]
+[[Category: Large Structures]]
-[[Category: Fermani, S]]
+[[Category: Falini G]]
-[[Category: Marri, L]]
+[[Category: Fermani S]]
-[[Category: Sparla, F]]
+[[Category: Marri L]]
-[[Category: Thumiger, A]]
+[[Category: Sparla F]]
-[[Category: Trost, P]]
+[[Category: Thumiger A]]
-[[Category: Calvin cycle]]
+[[Category: Trost P]]
-[[Category: Chloroplast]]
-[[Category: Nad]]
-[[Category: Oxidoreductase-protein binding complex]]
-[[Category: Rossmann fold]]

3qv1

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Crystal structure of the binary complex of photosyntetic A4 glyceraldehyde 3-phosphate dehydrogenase (GAPDH) with cp12-2, both from Arabidopsis thaliana.

Structural highlights

Function

See Also

Contents

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