5xww

Substrate-bound Structure of G355T/Q364H mutant of a Ketoreductase from amphotericin Polyketide Synthases

spinqualitylabelsall models 5xww, resolution 1.96Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5xww is a 2 chain structure with sequence from Streptomyces nodosus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.96Å Ligands: 8H6, NAP Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q93NW7_9ACTN Publication Abstract from PubMed Ketoreductase (KR) domains of modular polyketide synthases (PKSs) control the stereochemistry of C2 methyl and C3 hydroxyl substituents of polyketide intermediates. To understand the molecular basis of stereocontrol exerted by KRs, the crystal structure of a KR from the second module of the amphotericin PKS (AmpKR2) complexed with NADP(+) and 2-methyl-3-oxopentanoyl-pantetheine was solved. This first ternary structure provides direct evidence to the hypothesis that a substrate enters into the active site of an A-type KR from the side opposite the coenzyme to generate an L-hydroxyl substituent. A comparison with the ternary complex of a G355T/Q364H mutant sheds light on the structural basis for stereospecificity toward the substrate C2 methyl substituent. Functional assays suggest the pantetheine handle shows obvious influence on the catalytic efficiency and the stereochemical outcome. Together, these findings extend our current understanding of the stereochemical control of PKS KR domains. Substrate-bound structures of a ketoreductase from amphotericin modular polyketide synthase.,Liu C, Yuan M, Xu X, Wang L, Keatinge-Clay AT, Deng Z, Lin S, Zheng J J Struct Biol. 2018 Apr 4. pii: S1047-8477(18)30091-1. doi:, 10.1016/j.jsb.2018.04.001. PMID:29626512 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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