1sqc
From Proteopedia
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|PDB= 1sqc |SIZE=350|CAPTION= <scene name='initialview01'>1sqc</scene>, resolution 2.85Å | |PDB= 1sqc |SIZE=350|CAPTION= <scene name='initialview01'>1sqc</scene>, resolution 2.85Å | ||
|SITE= <scene name='pdbsite=LDA:The+Active+Site+Is+Located+In+A+Large+Central+Cavity,+As+...'>LDA</scene> | |SITE= <scene name='pdbsite=LDA:The+Active+Site+Is+Located+In+A+Large+Central+Cavity,+As+...'>LDA</scene> | ||
| - | |LIGAND= <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene> | + | |LIGAND= <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
[[Category: Wendt, K U.]] | [[Category: Wendt, K U.]] | ||
| - | [[Category: LDA]] | ||
[[Category: 29-ene) and diplopterol (hopane-22-ol)]] | [[Category: 29-ene) and diplopterol (hopane-22-ol)]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
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[[Category: terpenoid metabolism]] | [[Category: terpenoid metabolism]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:45:36 2008'' |
Revision as of 20:45, 30 March 2008
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| , resolution 2.85Å | |||||||
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| Sites: | |||||||
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 23:45:36 2008
