1qfl
From Proteopedia
(New page: 200px<br /> <applet load="1qfl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qfl, resolution 1.92Å" /> '''BIOSYNTHETIC THIOLA...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1QFL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera]] with SO4 and COA 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=2.3.1.9 2.3.1.9]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFL OCA]]. | + | 1QFL is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Zoogloea_ramigera Zoogloea ramigera]] with SO4 and COA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Active as [[http://en.wikipedia.org/wiki/Acetyl-CoA_C-acetyltransferase Acetyl-CoA C-acetyltransferase]], with EC number [[http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.1.9 2.3.1.9]]. Structure known Active Sites: AS1, AS2, AS3 and AS4. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QFL OCA]]. |
==Reference== | ==Reference== | ||
A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism., Modis Y, Wierenga RK, Structure. 1999 Oct 15;7(10):1279-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545327 10545327] | A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism., Modis Y, Wierenga RK, Structure. 1999 Oct 15;7(10):1279-90. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10545327 10545327] | ||
| + | [[Category: Acetyl-CoA C-acetyltransferase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Zoogloea ramigera]] | [[Category: Zoogloea ramigera]] | ||
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[[Category: thiolase]] | [[Category: thiolase]] | ||
| - | ''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 10:57:09 2007'' |
Revision as of 08:52, 30 October 2007
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BIOSYNTHETIC THIOLASE FROM ZOOGLOEA RAMIGERA IN COMPLEX WITH A REACTION INTERMEDIATE.
Overview
BACKGROUND: Thiolases are ubiquitous and form a large family of dimeric or, tetrameric enzymes with a conserved, five-layered alphabetaalphabetaalpha, catalytic domain. Thiolases can function either degradatively, in the, beta-oxidation pathway of fatty acids, or biosynthetically. Biosynthetic, thiolases catalyze the biological Claisen condensation of two molecules of, acetyl-CoA to form acetoacetyl-CoA. This is one of the fundamental, categories of carbon skeletal assembly patterns in biological systems and, is the first step in a wide range of biosynthetic pathways, including, those that generate cholesterol, steroid hormones, and various, energy-storage molecules. RESULTS: The crystal structure of the tetrameric, biosynthetic thiolase from Zoogloea ramigera has been determined at 2.0 ... [(full description)]
About this Structure
1QFL is a [Single protein] structure of sequence from [Zoogloea ramigera] with SO4 and COA as [ligands]. Active as [Acetyl-CoA C-acetyltransferase], with EC number [2.3.1.9]. Structure known Active Sites: AS1, AS2, AS3 and AS4. Full crystallographic information is available from [OCA].
Reference
A biosynthetic thiolase in complex with a reaction intermediate: the crystal structure provides new insights into the catalytic mechanism., Modis Y, Wierenga RK, Structure. 1999 Oct 15;7(10):1279-90. PMID:10545327
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