1UMP
GEOMETRY OF TRITERPENE CONVERSION TO PENTACARBOCYCLIC HOPENE
Summary for 1UMP
| Entry DOI | 10.2210/pdb1ump/pdb |
| Related | 1GSZ 1H35 1H36 1H37 1H39 1H3A 1H3B 1H3C 1O6H 1O6Q 1O6R 1O79 1SQC 2SQC 3SQC |
| Descriptor | SQUALENE--HOPENE CYCLASE, (HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE, 2-AZASQUALENE, ... (4 entities in total) |
| Functional Keywords | isomerase, triterpene cyclase, cholesterol biosynthesis, oxidosqualene cyclase, monotopic membrane protein |
| Biological source | ALICYCLOBACILLUS ACIDOCALDARIUS (ALICYCLOBACILLUS ACIDOCALDARIUS) |
| Total number of polymer chains | 3 |
| Total formula weight | 217723.47 |
| Authors | Reinert, D.J.,Balliano, G.,Schulz, G.E. (deposition date: 2003-08-27, release date: 2004-02-03, Last modification date: 2023-12-13) |
| Primary citation | Reinert, D.J.,Balliano, G.,Schulz, G.E. Conversion of Squalene to the Pentacarbocyclic Hopene Chem.Biol., 11:121-, 2004 Cited by PubMed Abstract: 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. PubMed: 15113001DOI: 10.1016/J.CHEMBIOL.2003.12.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.13 Å) |
Structure validation
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