1sqc
From Proteopedia
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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 coupled to a histidine. Numerous surface alpha helices, are connected by characteristic QW-motifs (Q is glutamine and W is, tryptophan) that tighten the protein structure, possibly for absorbing the, reaction energy without structural damage.
About this Structure
1SQC is a Single protein structure of sequence from Alicyclobacillus acidocaldarius with LDA as ligand. Known structural/functional Site: . 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
Page seeded by OCA on Tue Dec 18 18:00:56 2007
