1ump
From Proteopedia
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|PDB= 1ump |SIZE=350|CAPTION= <scene name='initialview01'>1ump</scene>, resolution 2.13Å | |PDB= 1ump |SIZE=350|CAPTION= <scene name='initialview01'>1ump</scene>, resolution 2.13Å | ||
|SITE= <scene name='pdbsite=AC1:Sqa+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Sqa+Binding+Site+For+Chain+C'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene> | + | |LIGAND= <scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=SQA:2-AZASQUALENE'>SQA</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Squalene--hopene_cyclase Squalene--hopene cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.17 5.4.99.17] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Squalene--hopene_cyclase Squalene--hopene cyclase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.4.99.17 5.4.99.17] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ump FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ump OCA], [http://www.ebi.ac.uk/pdbsum/1ump PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ump RCSB]</span> | ||
}} | }} | ||
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[[Category: Reinert, D J.]] | [[Category: Reinert, D J.]] | ||
[[Category: Schulz, G E.]] | [[Category: Schulz, G E.]] | ||
| - | [[Category: C8E]] | ||
| - | [[Category: SQA]] | ||
[[Category: cholesterol biosynthesis]] | [[Category: cholesterol biosynthesis]] | ||
[[Category: isomerase]] | [[Category: isomerase]] | ||
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[[Category: triterpene cyclase]] | [[Category: triterpene cyclase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:12:26 2008'' |
Revision as of 21:12, 30 March 2008
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| , resolution 2.13Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , | ||||||
| Activity: | Squalene--hopene cyclase, with EC number 5.4.99.17 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE
Overview
The membrane protein squalene-hopene cyclase was cocrystallized with 2-azasqualene and analyzed by X-ray diffraction to 2.13 A resolution. The conformation of this close analog was clearly established, and it agreed with the common textbook presentation. The bound squalene undergoes only small conformational changes during the formation of rings A through D, thus requiring no intermediate. However, ring E formation is hindered by an entropic barrier, which may explain its absence in the steroids. The structure analysis revealed a mobile region between the active center cavity and the membrane, which may melt, opening a passage for squalene and hopene.
About this Structure
1UMP is a Single protein structure of sequence from Alicyclobacillus acidocaldarius. Full crystallographic information is available from OCA.
Reference
Conversion of squalene to the pentacarbocyclic hopene., Reinert DJ, Balliano G, Schulz GE, Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001
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