6K97
Crystal structure of fusion DH domain
Summary for 6K97
| Entry DOI | 10.2210/pdb6k97/pdb |
| Descriptor | Fusion DH, SULFATE ION (3 entities in total) |
| Functional Keywords | double hot dog fold, polyketide synthase, dehydratase, cremimycin biosynthesis, lyase |
| Biological source | Streptomyces sp. MJ635-86F5 More |
| Total number of polymer chains | 2 |
| Total formula weight | 70764.75 |
| Authors | Kawasaki, D.,Miyanaga, A.,Chisuga, T.,Kudo, F.,Eguchi, T. (deposition date: 2019-06-14, release date: 2019-11-27, Last modification date: 2023-11-22) |
| Primary citation | Kawasaki, D.,Miyanaga, A.,Chisuga, T.,Kudo, F.,Eguchi, T. Functional and Structural Analyses of the Split-Dehydratase Domain in the Biosynthesis of Macrolactam Polyketide Cremimycin. Biochemistry, 58:4799-4803, 2019 Cited by PubMed Abstract: In the biosynthesis of the macrolactam antibiotic cremimycin, the 3-aminononanoic acid starter unit is formed via a non-2-enoyl acyl carrier protein thioester intermediate, which is presumed to be constructed by -acyltransferase (AT) polyketide synthases (PKSs) CmiP2, CmiP3, and CmiP4. While canonical -AT PKS modules are comprised of a single polypeptide, the PKS module formed by CmiP2 and CmiP3 is split within the dehydratase (DH) domain. Here, we report the enzymatic function and the structural features of this split-DH domain. analysis showed that the split-DH domain catalyzes the dehydration reaction of ()-3-hydroxynonanoyl -acetylcysteamine thioester (SNAC) to form ()-non-2-enoyl-SNAC, suggesting that the split-DH domain is catalytically active in cremimycin biosynthesis. In addition, structural analysis revealed that the CmiP2 and CmiP3 subunits of the split-DH domain form a tightly associated heterodimer through several hydrogen bonding and hydrophobic interactions, which are similar to those of canonical DH domains of other -AT PKSs. These results indicate that the split-DH domain has the same function and structure as common -AT PKS DH domains. PubMed: 31721563DOI: 10.1021/acs.biochem.9b00897 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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