5HMC
Crystal structure of S. sahachiroi AziG complexed with 5-methyl naphthoic acid
Summary for 5HMC
| Entry DOI | 10.2210/pdb5hmc/pdb |
| Related | 5HMB |
| Descriptor | Azi13, 5-methylnaphthalene-1-carboxylic acid, SULFATE ION, ... (4 entities in total) |
| Functional Keywords | azinomycin biosynthesis, polyketide synthase, thioesterase, naphthoate, hydrolase |
| Biological source | Streptomyces sahachiroi |
| Total number of polymer chains | 1 |
| Total formula weight | 15794.55 |
| Authors | Zhang, Y.,Erb, M.S.,Ealick, S.E. (deposition date: 2016-01-15, release date: 2016-02-03, Last modification date: 2024-04-03) |
| Primary citation | Mori, S.,Simkhada, D.,Zhang, H.,Erb, M.S.,Zhang, Y.,Williams, H.,Fedoseyenko, D.,Russell, W.K.,Kim, D.,Fleer, N.,Ealick, S.E.,Watanabe, C.M. Polyketide Ring Expansion Mediated by a Thioesterase, Chain Elongation and Cyclization Domain, in Azinomycin Biosynthesis: Characterization of AziB and AziG. Biochemistry, 55:704-714, 2016 Cited by PubMed Abstract: The azinomycins are a family of potent antitumor agents with the ability to form interstrand cross-links with DNA. This study reports on the unusual biosynthetic formation of the 5-methyl naphthoate moiety, which is essential for effective DNA association. While sequence analysis predicts that the polyketide synthase (AziB) catalyzes the formation of this naphthoate, 2-methylbenzoic acid, a truncated single-ring product, is formed instead. We demonstrate that the thioesterase (AziG) acts as a chain elongation and cyclization (CEC) domain and is required for the additional two rounds of chain extension to form the expected product. PubMed: 26731610DOI: 10.1021/acs.biochem.5b01050 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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