7S6B
Crystal structure of modular polyketide synthase apo-Lsd14 from the Lasalocid biosynthesis pathway, trapped in the transacylation step
Summary for 7S6B
| Entry DOI | 10.2210/pdb7s6b/pdb |
| Descriptor | Polyketide synthase, ... (4 entities in total) |
| Functional Keywords | modular polyketide synthase, ketosynthase, acyltransferase, acyl carrier protein, biosynthetic protein |
| Biological source | Streptomyces lasalocidi More |
| Total number of polymer chains | 5 |
| Total formula weight | 332236.98 |
| Authors | Bagde, S.R.,Mathews, I.I.,Kim, C.-Y. (deposition date: 2021-09-13, release date: 2021-11-03, Last modification date: 2024-05-22) |
| Primary citation | Bagde, S.R.,Mathews, I.I.,Fromme, J.C.,Kim, C.Y. Modular polyketide synthase contains two reaction chambers that operate asynchronously. Science, 374:723-729, 2021 Cited by PubMed Abstract: Type I modular polyketide synthases are homodimeric multidomain assembly line enzymes that synthesize a variety of polyketide natural products by performing polyketide chain extension and β-keto group modification reactions. We determined the 2.4-angstrom-resolution x-ray crystal structure and the 3.1-angstrom-resolution cryo–electron microscopy structure of the Lsd14 polyketide synthase, stalled at the transacylation and condensation steps, respectively. These structures revealed how the constituent domains are positioned relative to each other, how they rearrange depending on the step in the reaction cycle, and the specific interactions formed between the domains. Like the evolutionarily related mammalian fatty acid synthase, Lsd14 contains two reaction chambers, but only one chamber in Lsd14 has the full complement of catalytic domains, indicating that only one chamber produces the polyketide product at any given time. PubMed: 34735234DOI: 10.1126/science.abi8532 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.35 Å) |
Structure validation
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