6B2V
Pyran synthase domain from module nine of the sorangicin pathway
Summary for 6B2V
| Entry DOI | 10.2210/pdb6b2v/pdb |
| Descriptor | SorB (2 entities in total) |
| Functional Keywords | polyketide, pyran, trans-at, antibiotic, transferase |
| Biological source | Sorangium cellulosum |
| Total number of polymer chains | 1 |
| Total formula weight | 32801.00 |
| Authors | Wagner, D.T.,Keatinge-Clay, A.T. (deposition date: 2017-09-20, release date: 2018-04-18, Last modification date: 2024-03-13) |
| Primary citation | Wagner, D.T.,Zhang, Z.,Meoded, R.A.,Cepeda, A.J.,Piel, J.,Keatinge-Clay, A.T. Structural and Functional Studies of a Pyran Synthase Domain from a trans-Acyltransferase Assembly Line. ACS Chem. Biol., 13:975-983, 2018 Cited by PubMed Abstract: trans-Acyltransferase assembly lines possess enzymatic domains often not observed in their better characterized cis-acyltransferase counterparts. Within this repertoire of largely unexplored biosynthetic machinery is a class of enzymes called the pyran synthases that catalyze the formation of five- and six-membered cyclic ethers from diverse polyketide chains. The 1.55 Å resolution crystal structure of a pyran synthase domain excised from the ninth module of the sorangicin assembly line highlights the similarity of this enzyme to the ubiquitous dehydratase domain and provides insight into the mechanism of ring formation. Functional assays of point mutants reveal the central importance of the active site histidine that is shared with the dehydratases as well as the supporting role of a neighboring semiconserved asparagine. PubMed: 29481043DOI: 10.1021/acschembio.8b00049 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.55 Å) |
Structure validation
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