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1qfl
From Proteopedia
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[[Category: thiolase]] | [[Category: thiolase]] | ||
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Revision as of 13:54, 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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