Structural highlights
Function
SQHC_ALIAD Catalyzes the cyclization of squalene into hopene.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Conversion of squalene to the pentacarbocyclic hopene.,Reinert DJ, Balliano G, Schulz GE Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Reinert DJ, Balliano G, Schulz GE. Conversion of squalene to the pentacarbocyclic hopene. Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001 doi:http://dx.doi.org/10.1016/j.chembiol.2003.12.013
