5czd | pdb_00005czd

The complex structure of VinK with VinL

spinqualitylabelsall models 5czd, resolution 2.34Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5czd is a 2 chain structure with sequence from "actinomyces_halstedii"_waksman_and_curtis_1916 "actinomyces halstedii" waksman and curtis 1916. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 1N2, PNS Related: 5czc Gene: vinK ("Actinomyces halstedii" Waksman and Curtis 1916), vinL ("Actinomyces halstedii" Waksman and Curtis 1916) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Acyltransferases (ATs) are key determinants of building block specificity in polyketide biosynthesis. Despite the importance of protein-protein interactions between AT and acyl carrier protein (ACP) during the acyltransfer reaction, the mechanism of ACP recognition by AT is not understood in detail. Herein, we report the crystal structure of AT VinK, which transfers a dipeptide group between two ACPs, VinL and VinP1LdACP, in vicenistatin biosynthesis. The isolated VinK structure showed a unique substrate-binding pocket for the dipeptide group linked to ACP. To gain greater insight into the mechanism of ACP recognition, we attempted to crystallize the VinK-ACP complexes. Because transient enzyme-ACP complexes are difficult to crystallize, we developed a covalent cross-linking strategy using a bifunctional maleimide reagent to trap the VinK-ACP complexes, allowing the determination of the crystal structure of the VinK-VinL complex. In the complex structure, Arg-153, Met-206, and Arg-299 of VinK interact with the negatively charged helix II region of VinL. The VinK-VinL complex structure allows, to our knowledge, the first visualization of the interaction between AT and ACP and provides detailed mechanistic insights into ACP recognition by AT. Structure-based analysis of the molecular interactions between acyltransferase and acyl carrier protein in vicenistatin biosynthesis.,Miyanaga A, Iwasawa S, Shinohara Y, Kudo F, Eguchi T Proc Natl Acad Sci U S A. 2016 Feb 16;113(7):1802-7. doi:, 10.1073/pnas.1520042113. Epub 2016 Feb 1. PMID:26831085 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein 3D structures

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