3V1V
Crystal structure of 2-methylisoborneol synthase from Streptomyces coelicolor A3(2) in complex with Mg2+ and geranyl-S-thiolodiphosphate
Summary for 3V1V
| Entry DOI | 10.2210/pdb3v1v/pdb |
| Related | 3V1X |
| Descriptor | 2-methylisoborneol synthase, MAGNESIUM ION, GERANYL S-THIOLODIPHOSPHATE, ... (5 entities in total) |
| Functional Keywords | class i terpenoid cyclase fold, ddxxxxd motif, ndxxsxxxe motif, 2-methylisoborneol biosynthesis, biosynthesis of 2-methylisoborneol, lyase |
| Biological source | Streptomyces coelicolor |
| Total number of polymer chains | 1 |
| Total formula weight | 47865.85 |
| Authors | Koksal, M.,Christianson, D.W. (deposition date: 2011-12-10, release date: 2012-04-11, Last modification date: 2024-02-28) |
| Primary citation | Koksal, M.,Chou, W.K.,Cane, D.E.,Christianson, D.W. Structure of 2-Methylisoborneol Synthase from Streptomyces coelicolor and Implications for the Cyclization of a Noncanonical C-Methylated Monoterpenoid Substrate. Biochemistry, 51:3011-3020, 2012 Cited by PubMed Abstract: The crystal structure of 2-methylisoborneol synthase (MIBS) from Streptomyces coelicolor A3(2) has been determined in complex with substrate analogues geranyl-S-thiolodiphosphate and 2-fluorogeranyl diphosphate at 1.80 and 1.95 Å resolution, respectively. This terpenoid cyclase catalyzes the cyclization of the naturally occurring, noncanonical C-methylated isoprenoid substrate, 2-methylgeranyl diphosphate, to form the bicyclic product 2-methylisoborneol, a volatile C(11) homoterpene alcohol with an earthy, musty odor. While MIBS adopts the tertiary structure of a class I terpenoid cyclase, its dimeric quaternary structure differs from that previously observed in dimeric terpenoid cyclases from plants and fungi. The quaternary structure of MIBS is nonetheless similar in some respects to that of dimeric farnesyl diphosphate synthase, which is not a cyclase. The structures of MIBS complexed with substrate analogues provide insights regarding differences in the catalytic mechanism of MIBS and the mechanisms of (+)-bornyl diphosphate synthase and endo-fenchol synthase, plant cyclases that convert geranyl diphosphate into products with closely related bicyclic bornyl skeletons, but distinct structures and stereochemistries. PubMed: 22455514DOI: 10.1021/bi201827a PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
