1jqn
From Proteopedia
(New page: 200px<br /><applet load="1jqn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqn, resolution 2.35Å" /> '''Crystal structure of...) |
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| - | [[Image:1jqn.gif|left|200px]]<br /><applet load="1jqn" size=" | + | [[Image:1jqn.gif|left|200px]]<br /><applet load="1jqn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jqn, resolution 2.35Å" /> | caption="1jqn, resolution 2.35Å" /> | ||
'''Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP'''<br /> | '''Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Phosphoenolpyruvate carboxylase (PEPC) catalyzes the first step in the | + | Phosphoenolpyruvate 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1JQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with MN, ASP and DCO as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 1JQN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=MN:'>MN</scene>, <scene name='pdbligand=ASP:'>ASP</scene> and <scene name='pdbligand=DCO:'>DCO</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JQN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: mn2+ and dcdp complex]] | [[Category: mn2+ and dcdp complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:37 2008'' |
Revision as of 11:25, 21 February 2008
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Crystal structure of E.coli phosphoenolpyruvate carboxylase in complex with Mn2+ and DCDP
Overview
Phosphoenolpyruvate 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.
About this Structure
1JQN is a Single protein structure of sequence from Escherichia coli with , and as ligands. Active as Phosphoenolpyruvate carboxylase, with EC number 4.1.1.31 Full crystallographic information is available from OCA.
Reference
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
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