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1sqc

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[[Image:1sqc.jpg|left|200px]]
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{{Structure
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|PDB= 1sqc |SIZE=350|CAPTION= <scene name='initialview01'>1sqc</scene>, resolution 2.85&Aring;
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|SITE= <scene name='pdbsite=LDA:The+Active+Site+Is+Located+In+A+Large+Central+Cavity,+As+...'>LDA</scene>
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{{STRUCTURE_1sqc| PDB=1sqc | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1sqc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sqc OCA], [http://www.ebi.ac.uk/pdbsum/1sqc PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1sqc RCSB]</span>
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'''SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS'''
'''SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS'''
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[[Category: Schulz, G E.]]
[[Category: Schulz, G E.]]
[[Category: Wendt, K U.]]
[[Category: Wendt, K U.]]
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[[Category: 29-ene) and diplopterol (hopane-22-ol)]]
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[[Category: Isomerase]]
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[[Category: isomerase]]
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[[Category: Membrane protein]]
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[[Category: membrane protein]]
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[[Category: Terpenoid metabolism]]
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[[Category: squalene to hopene (hop-22]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:00:54 2008''
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[[Category: terpenoid metabolism]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:36 2008''
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Revision as of 06:00, 3 May 2008

Template:STRUCTURE 1sqc

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. 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 Sat May 3 09:00:54 2008

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