2c31
From Proteopedia
(New page: 200px<br /> <applet load="2c31" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c31, resolution 1.73Å" /> '''CRYSTAL STRUCTURE O...) |
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==About this Structure== | ==About this Structure== | ||
| - | 2C31 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]] with MG, TZD and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/ ]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.8 4.1.1.8]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C31 OCA]]. | + | 2C31 is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Oxalobacter_formigenes Oxalobacter formigenes]] with MG, TZD and ADP as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Oxalyl-CoA_decarboxylase Oxalyl-CoA decarboxylase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.1.1.8 4.1.1.8]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C31 OCA]]. |
==Reference== | ==Reference== | ||
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate., Berthold CL, Moussatche P, Richards NG, Lindqvist Y, J Biol Chem. 2005 Dec 16;280(50):41645-54. Epub 2005 Oct 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16216870 16216870] | Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate., Berthold CL, Moussatche P, Richards NG, Lindqvist Y, J Biol Chem. 2005 Dec 16;280(50):41645-54. Epub 2005 Oct 10. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16216870 16216870] | ||
[[Category: Oxalobacter formigenes]] | [[Category: Oxalobacter formigenes]] | ||
| + | [[Category: Oxalyl-CoA decarboxylase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Berthold, C.L.]] | [[Category: Berthold, C.L.]] | ||
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[[Category: thiamine pyrophosphate]] | [[Category: thiamine pyrophosphate]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:11:39 2007'' |
Revision as of 10:06, 30 October 2007
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CRYSTAL STRUCTURE OF OXALYL-COA DECARBOXYLASE IN COMPLEX WITH THE COFACTOR DERIVATIVE THIAMIN-2-THIAZOLONE DIPHOSPHATE AND ADENOSINE DIPHOSPHATE
Overview
Oxalyl-coenzyme A decarboxylase is a thiamin diphosphate-dependent enzyme, that plays an important role in the catabolism of the highly toxic, compound oxalate. We have determined the crystal structure of the enzyme, from Oxalobacter formigenes from a hemihedrally twinned crystal to 1.73 A, resolution and characterized the steady-state kinetic behavior of the, decarboxylase. The monomer of the tetrameric enzyme consists of three, alpha/beta-type domains, commonly seen in this class of enzymes, and the, thiamin diphosphate-binding site is located at the expected, subunit-subunit interface between two of the domains with the cofactor, bound in the conserved V-conformation. Although oxalyl-CoA decarboxylase, is structurally homologous to acetohydroxyacid synthase, a molecule of ADP, is bound ... [(full description)]
About this Structure
2C31 is a [Single protein] structure of sequence from [Oxalobacter formigenes] with MG, TZD and ADP as [ligands]. Active as [Oxalyl-CoA decarboxylase], with EC number [4.1.1.8]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Structural basis for activation of the thiamin diphosphate-dependent enzyme oxalyl-CoA decarboxylase by adenosine diphosphate., Berthold CL, Moussatche P, Richards NG, Lindqvist Y, J Biol Chem. 2005 Dec 16;280(50):41645-54. Epub 2005 Oct 10. PMID:16216870
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