1sqc
From Proteopedia
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- | [[Image:1sqc.jpg|left|200px]] | + | [[Image:1sqc.jpg|left|200px]] |
- | + | ||
- | '''SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS''' | + | {{Structure |
+ | |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> | ||
+ | |LIGAND= <scene name='pdbligand=LDA:LAURYL DIMETHYLAMINE-N-OXIDE'>LDA</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''SQUALENE-HOPENE-CYCLASE FROM ALICYCLOBACILLUS ACIDOCALDARIUS''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1SQC is a [ | + | 1SQC is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Alicyclobacillus_acidocaldarius Alicyclobacillus acidocaldarius]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SQC OCA]. |
==Reference== | ==Reference== | ||
- | Structure and function of a squalene cyclase., Wendt KU, Poralla K, Schulz GE, Science. 1997 Sep 19;277(5333):1811-5. PMID:[http:// | + | Structure and function of a squalene cyclase., Wendt KU, Poralla K, Schulz GE, Science. 1997 Sep 19;277(5333):1811-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9295270 9295270] |
[[Category: Alicyclobacillus acidocaldarius]] | [[Category: Alicyclobacillus acidocaldarius]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: terpenoid metabolism]] | [[Category: terpenoid metabolism]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:08:16 2008'' |
Revision as of 12:08, 20 March 2008
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, resolution 2.85Å | |||||||
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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
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