1jqo
From Proteopedia
(New page: 200px<br /><applet load="1jqo" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jqo, resolution 3.00Å" /> '''Crystal structure of...) |
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| - | [[Image:1jqo.jpg|left|200px]]<br /><applet load="1jqo" size=" | + | [[Image:1jqo.jpg|left|200px]]<br /><applet load="1jqo" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1jqo, resolution 3.00Å" /> | caption="1jqo, resolution 3.00Å" /> | ||
'''Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize'''<br /> | '''Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize'''<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== | ||
| - | 1JQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | + | 1JQO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Zea_mays Zea mays] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=1JQO OCA]. |
==Reference== | ==Reference== | ||
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[[Category: carbon dioxide fixation]] | [[Category: carbon dioxide fixation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:25:43 2008'' |
Revision as of 11:25, 21 February 2008
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Crystal structure of C4-form phosphoenolpyruvate carboxylase from maize
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
1JQO is a Single protein structure of sequence from Zea mays with as ligand. 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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