5XK7
Crystal structure of Isosesquilavandulyl Diphosphate Synthase from Streptomyces sp. strain CNH-189 in complex with DMAPP
Summary for 5XK7
| Entry DOI | 10.2210/pdb5xk7/pdb |
| Related | 5XK3 5XK6 5XK8 5XK9 |
| Descriptor | Undecaprenyl diphosphate synthase, MAGNESIUM ION, PYROPHOSPHATE 2-, ... (7 entities in total) |
| Functional Keywords | prenyltransferase, antibiotic biosynthesis, transferase |
| Biological source | Streptomyces sp. CNH189 |
| Total number of polymer chains | 4 |
| Total formula weight | 109521.23 |
| Authors | Ko, T.P.,Guo, R.T.,Liu, W.,Chen, C.C.,Gao, J. (deposition date: 2017-05-05, release date: 2018-01-10, Last modification date: 2023-11-22) |
| Primary citation | Gao, J.,Ko, T.P.,Chen, L.,Malwal, S.R.,Zhang, J.,Hu, X.,Qu, F.,Liu, W.,Huang, J.W.,Cheng, Y.S.,Chen, C.C.,Yang, Y.,Zhang, Y.,Oldfield, E.,Guo, R.T. "Head-to-Middle" and "Head-to-Tail" cis-Prenyl Transferases: Structure of Isosesquilavandulyl Diphosphate Synthase. Angew. Chem. Int. Ed. Engl., 57:683-687, 2018 Cited by PubMed Abstract: We report the first X-ray crystallographic structure of the "head-to-middle" prenyltransferase, isosesquilavandulyl diphosphate synthase, involved in biosynthesis of the merochlorin class of antibiotics. The protein adopts the ζ or cis-prenyl transferase fold but remarkably, unlike tuberculosinol adenosine synthase and other cis-prenyl transferases (e.g. cis-farnesyl, decaprenyl, undecaprenyl diphosphate synthases), the large, hydrophobic side chain does not occupy a central hydrophobic tunnel. Instead, it occupies a surface pocket oriented at 90° to the hydrophobic tunnel. Product chain-length control is achieved by squeezing out the ligand from the conventional allylic S1 binding site, with proton abstraction being achieved using a diphosphate-Asn-Ser relay. The structures revise and unify our thinking as to the mechanism of action of many other prenyl transferases and may also be of use in engineering new merochlorin-class antibiotics. PubMed: 29215779DOI: 10.1002/anie.201710185 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.911 Å) |
Structure validation
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