1ump | pdb_00001ump

GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE

spinqualitylabelsall models 1ump, resolution 2.13Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ump is a 3 chain structure with sequence from Alicyclobacillus acidocaldarius. The December 2007 RCSB PDB Molecule of the Month feature on Oxidosqualene Cyclase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2007_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.13Å Ligands: C8E, SQA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Squalene-hopene cyclase

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