1qfl
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(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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Revision as of 14:57, 29 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 [[1]], with EC number [2.3.1.9]. 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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