7f2r | pdb_00007f2r

Crystal structure of VinK-VinL covalent complex formed with a pantetheineamide cross-linking probe

spinqualitylabelsall models 7f2r, resolution 1.95Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7f2r is a 4 chain structure with sequence from Streptomyces halstedii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.95Å Ligands: 9EF Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q76KY5_STRHA Publication Abstract from PubMed Acyltransferases are responsible for the selection and loading of acyl units onto carrier proteins in polyketide and fatty-acid biosynthesis. Despite the importance of protein-protein interactions between the acyltransferase and the carrier protein, structural information on acyltransferase-carrier protein interactions is limited because of the transient interactions between them. In the biosynthesis of the polyketide vicenistatin, the acyltransferase VinK recognizes the carrier protein VinL for the transfer of a dipeptidyl unit. The crystal structure of a VinK-VinL covalent complex formed with a 1,2-bismaleimidoethane cross-linking reagent has been determined previously. Here, the crystal structure of a VinK-VinL covalent complex formed with a pantetheine cross-linking probe is reported at 1.95 A resolution. In the structure of the VinK-VinL-probe complex, the pantetheine probe that is attached to VinL is covalently connected to the side chain of the mutated Cys106 of VinK. The interaction interface between VinK and VinL is essentially the same in the two VinK-VinL complex structures, although the position of the pantetheine linker slightly differs. This structural observation suggests that interface interactions are not affected by the cross-linking strategy used. Complex structure of the acyltransferase VinK and the carrier protein VinL with a pantetheine cross-linking probe.,Miyanaga A, Ouchi R, Kudo F, Eguchi T Acta Crystallogr F Struct Biol Commun. 2021 Sep 1;77(Pt 9):294-302. doi:, 10.1107/S2053230X21008761. Epub 2021 Aug 26. PMID:34473106 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Acyl carrier protein 3D structures

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