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1cqj
From Proteopedia
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| - | [[Image:1cqj.png|left|200px]] | ||
| - | + | ==CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE== | |
| - | + | <StructureSection load='1cqj' size='340' side='right'caption='[[1cqj]], [[Resolution|resolution]] 2.90Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[1cqj]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CQJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CQJ FirstGlance]. <br> | |
| - | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9Å</td></tr> | |
| - | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></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=1cqj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cqj OCA], [https://pdbe.org/1cqj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cqj RCSB], [https://www.ebi.ac.uk/pdbsum/1cqj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cqj ProSAT]</span></td></tr> |
| - | [[1cqj]] is a 4 chain structure | + | </table> |
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/SUCD_ECOLI SUCD_ECOLI] During aerobic metabolism it functions in the citric acid cycle, coupling the hydrolysis of succinyl-CoA to the synthesis of ATP and thus represents an important site of substrate-level phosphorylation. It can also function in the other direction for anabolic purposes, and this may be particularly important for providing succinyl-CoA during anaerobic growth when the oxidative route from 2-oxoglutarate is severely repressed. The alpha-subunit binds CoA, as well as ATP and catalyzes phosphoryl transfer to one of its histidine residues. The complete active site is probably located in the region of alpha-beta contact. | ||
| + | == Evolutionary Conservation == | ||
| + | [[Image:Consurf_key_small.gif|200px|right]] | ||
| + | Check<jmol> | ||
| + | <jmolCheckbox> | ||
| + | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cq/1cqj_consurf.spt"</scriptWhenChecked> | ||
| + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
| + | <text>to colour the structure by Evolutionary Conservation</text> | ||
| + | </jmolCheckbox> | ||
| + | </jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cqj ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
==See Also== | ==See Also== | ||
*[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]] | *[[Succinyl-CoA synthetase|Succinyl-CoA synthetase]] | ||
| - | + | *[[Succinyl-CoA synthetase 3D structures|Succinyl-CoA synthetase 3D structures]] | |
| - | + | __TOC__ | |
| - | < | + | </StructureSection> |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: | + | [[Category: Bridger WA]] |
| - | [[Category: | + | [[Category: Fraser ME]] |
| - | [[Category: | + | [[Category: James MNG]] |
| - | [[Category: | + | [[Category: Joyce MA]] |
| - | [[Category: | + | [[Category: Wolodko WT]] |
| - | + | ||
| - | + | ||
Current revision
CRYSTAL STRUCTURE OF DEPHOSPHORYLATED E. COLI SUCCINYL-COA SYNTHETASE
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