1sqc
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(New page: 200px<br /> <applet load="1sqc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1sqc, resolution 2.85Å" /> '''SQUALENE-HOPENE-CYC...)
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Revision as of 16:07, 29 October 2007
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SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS
Overview
The crystal structure of squalene-hopene cyclase from Alicyclobacillus, acidocaldarius was determined at 2.9 angstrom resolution. The mechanism, and sequence of this cyclase are closely related to those of, 2,3-oxidosqualene cyclases that catalyze the cyclization step in, cholesterol biosynthesis. The structure reveals a membrane protein with, membrane-binding characteristics similar to those of prostaglandin-H2, synthase, the only other reported protein of this type. The active site of, the enzyme is located in a large central cavity that is of suitable size, to bind squalene in its required conformation and that is lined by, aromatic residues. The structure supports a mechanism in which the acid, starting the reaction by protonating a carbon-carbon double bond is an, aspartate that is ... [(full description)]
About this Structure
1SQC is a [Single protein] structure of sequence from [Alicyclobacillus acidocaldarius] with LDA as [ligand]. Full crystallographic information is available from [OCA].
Reference
Structure and function of a squalene cyclase., Wendt KU, Poralla K, Schulz GE, Science. 1997 Sep 19;277(5333):1811-5. PMID:9295270
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