7s6b

Crystal structure of modular polyketide synthase apo-Lsd14 from the Lasalocid biosynthesis pathway, trapped in the transacylation step

spinqualitylabelsall models 7s6b, resolution 2.35Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7s6b is a 5 chain structure with sequence from Streptomyces lasalocidi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.35Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function B6ZK67_STRLS Publication Abstract from PubMed 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 beta-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. Modular polyketide synthase contains two reaction chambers that operate asynchronously.,Bagde SR, Mathews II, Fromme JC, Kim CY Science. 2021 Nov 5;374(6568):723-729. doi: 10.1126/science.abi8532. Epub 2021 , Nov 4. PMID:34735234 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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