1ump
|
GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE
OverviewOverview
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 StructureAbout this Structure
1UMP is a [Single protein] structure of sequence from [Alicyclobacillus acidocaldarius] with C8E and SQA as [ligands]. Active as [Squalene--hopene cyclase], with EC number [5.4.99.17]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
ReferenceReference
Conversion of squalene to the pentacarbocyclic hopene., Reinert DJ, Balliano G, Schulz GE, Chem Biol. 2004 Jan;11(1):121-6. PMID:15113001
Page seeded by OCA on Tue Oct 30 16:06:11 2007