1jqo: Difference between revisions
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==Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize== | ==Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize== | ||
<StructureSection load='1jqo' size='340' side='right' caption='[[1jqo]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1jqo' size='340' side='right' caption='[[1jqo]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fiy|1fiy]], [[1jqn|1jqn]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1fiy|1fiy]], [[1jqn|1jqn]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoenolpyruvate_carboxylase Phosphoenolpyruvate carboxylase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.31 4.1.1.31] </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=1jqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqo OCA], [http://pdbe.org/1jqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jqo RCSB], [http://www.ebi.ac.uk/pdbsum/1jqo PDBsum]</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=1jqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jqo OCA], [http://pdbe.org/1jqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jqo RCSB], [http://www.ebi.ac.uk/pdbsum/1jqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jqo ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/1jqo_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/jq/1jqo_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1jqo" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1jqo" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 11:39, 17 January 2018
Crystal structure of C4-form phosphoenolpyruvate carboxylase from maizeCrystal structure of C4-form phosphoenolpyruvate carboxylase from maize
Structural highlights
Function[CAPP1_MAIZE] Through the carboxylation of phosphoenolpyruvate (PEP) it forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPhosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the fixation of atmospheric CO(2) during C(4) photosynthesis. The crystal structure of C(4) form maize PEPC (ZmPEPC), the first structure of the plant PEPCs, has been determined at 3.0 A resolution. The structure includes a sulfate ion at the plausible binding site of an allosteric activator, glucose 6-phosphate. The crystal structure of E. coli PEPC (EcPEPC) complexed with Mn(2+), phosphoenolpyruvate analog (3,3-dichloro-2-dihydroxyphosphinoylmethyl-2-propenoate), and an allosteric inhibitor, aspartate, has also been determined at 2.35 A resolution. Dynamic movements were found in the ZmPEPC structure, compared with the EcPEPC structure, around two loops near the active site. On the basis of these molecular structures, the mechanisms for the carboxylation reaction and for the allosteric regulation of PEPC are proposed. Crystal structures of C4 form maize and quaternary complex of E. coli phosphoenolpyruvate carboxylases.,Matsumura H, Xie Y, Shirakata S, Inoue T, Yoshinaga T, Ueno Y, Izui K, Kai Y Structure. 2002 Dec;10(12):1721-30. PMID:12467579[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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