2c3c: Difference between revisions
New page: left|200px<br /> <applet load="2c3c" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c3c, resolution 2.15Å" /> '''2.01 ANGSTROM X-RAY... |
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==About this Structure== | ==About this Structure== | ||
2C3C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]] with COM, FAD, NAP and ACN 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=1.8.1.5 1.8.1.5]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3C OCA]]. | 2C3C is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Xanthobacter_autotrophicus Xanthobacter autotrophicus]] with COM, FAD, NAP and ACN as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/2-oxopropyl-CoM_reductase_(carboxylating) 2-oxopropyl-CoM reductase (carboxylating)]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.8.1.5 1.8.1.5]]. Structure known Active Site: AC1. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2C3C OCA]]. | ||
==Reference== | ==Reference== | ||
Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16388586 16388586] | Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16388586 16388586] | ||
[[Category: 2-oxopropyl-CoM reductase (carboxylating)]] | |||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Xanthobacter autotrophicus]] | [[Category: Xanthobacter autotrophicus]] | ||
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[[Category: redox-active center]] | [[Category: redox-active center]] | ||
''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 12:12:35 2007'' | ||
Revision as of 13:07, 30 October 2007
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2.01 ANGSTROM X-RAY CRYSTAL STRUCTURE OF A MIXED DISULFIDE BETWEEN COENZYME M AND NADPH-DEPENDENT OXIDOREDUCTASE 2-KETOPROPYL COENZYME M CARBOXYLASE
OverviewOverview
The structure of the mixed, enzyme-cofactor disulfide intermediate of, ketopropyl-coenzyme M oxidoreductase/carboxylase has been determined by, X-ray diffraction methods. Ketopropyl-coenzyme M, oxidoreductase/carboxylase belongs to a family of pyridine, nucleotide-containing flavin-dependent disulfide oxidoreductases, which, couple the transfer of hydride derived from the NADPH to the reduction of, protein cysteine disulfide. Ketopropyl-coenzyme M, oxidoreductase/carboxylase, a unique member of this enzyme class, catalyzes thioether bond cleavage of the substrate, 2-ketopropyl-coenzyme, M, and carboxylation of what is thought to be an enzyme-stabilized, enolacetone intermediate. The mixed disulfide of 2-ketopropyl-coenzyme M, oxidoreductase/carboxylase was captured through crystallization ... [(full description)]
About this StructureAbout this Structure
2C3C is a [Single protein] structure of sequence from [Xanthobacter autotrophicus] with COM, FAD, NAP and ACN as [ligands]. Active as [2-oxopropyl-CoM reductase (carboxylating)], with EC number [1.8.1.5]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Mechanistic implications of the structure of the mixed-disulfide intermediate of the disulfide oxidoreductase, 2-ketopropyl-coenzyme M oxidoreductase/carboxylase., Pandey AS, Nocek B, Clark DD, Ensign SA, Peters JW, Biochemistry. 2006 Jan 10;45(1):113-20. PMID:16388586
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