2nx9
From Proteopedia
(New page: 200px<br /><applet load="2nx9" size="350" color="white" frame="true" align="right" spinBox="true" caption="2nx9, resolution 1.70Å" /> '''Crystal structure of...) |
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==Overview== | ==Overview== | ||
| - | Oxaloacetate decarboxylase is a membrane-bound multiprotein complex that | + | Oxaloacetate decarboxylase is a membrane-bound multiprotein complex that couples oxaloacetate decarboxylation to sodium ion transport across the membrane. The initial reaction catalyzed by this enzyme machinery is the carboxyl transfer from oxaloacetate to the prosthetic biotin group. The crystal structure of the carboxyltransferase at 1.7 A resolution shows a dimer of alpha(8)beta(8) barrels with an active site metal ion, identified spectroscopically as Zn(2+), at the bottom of a deep cleft. The enzyme is completely inactivated by specific mutagenesis of Asp17, His207 and His209, which serve as ligands for the Zn(2+) metal ion, or by Lys178 near the active site, suggesting that Zn(2+) as well as Lys178 are essential for the catalysis. In the present structure this lysine residue is hydrogen-bonded to Cys148. A potential role of Lys178 as initial acceptor of the carboxyl group from oxaloacetate is discussed. |
==About this Structure== | ==About this Structure== | ||
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==Reference== | ==Reference== | ||
| - | Crystal | + | Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae., Studer R, Dahinden P, Wang WW, Auchli Y, Li XD, Dimroth P, J Mol Biol. 2007 Mar 23;367(2):547-57. Epub 2006 Dec 19. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17270211 17270211] |
[[Category: Oxaloacetate decarboxylase]] | [[Category: Oxaloacetate decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: zn2+ binding site]] | [[Category: zn2+ binding site]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:12:02 2008'' |
Revision as of 16:12, 21 February 2008
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Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae
Overview
Oxaloacetate decarboxylase is a membrane-bound multiprotein complex that couples oxaloacetate decarboxylation to sodium ion transport across the membrane. The initial reaction catalyzed by this enzyme machinery is the carboxyl transfer from oxaloacetate to the prosthetic biotin group. The crystal structure of the carboxyltransferase at 1.7 A resolution shows a dimer of alpha(8)beta(8) barrels with an active site metal ion, identified spectroscopically as Zn(2+), at the bottom of a deep cleft. The enzyme is completely inactivated by specific mutagenesis of Asp17, His207 and His209, which serve as ligands for the Zn(2+) metal ion, or by Lys178 near the active site, suggesting that Zn(2+) as well as Lys178 are essential for the catalysis. In the present structure this lysine residue is hydrogen-bonded to Cys148. A potential role of Lys178 as initial acceptor of the carboxyl group from oxaloacetate is discussed.
About this Structure
2NX9 is a Single protein structure of sequence from Vibrio cholerae with as ligand. Active as Oxaloacetate decarboxylase, with EC number 4.1.1.3 Full crystallographic information is available from OCA.
Reference
Crystal structure of the carboxyltransferase domain of the oxaloacetate decarboxylase Na+ pump from Vibrio cholerae., Studer R, Dahinden P, Wang WW, Auchli Y, Li XD, Dimroth P, J Mol Biol. 2007 Mar 23;367(2):547-57. Epub 2006 Dec 19. PMID:17270211
Page seeded by OCA on Thu Feb 21 18:12:02 2008
