5vdb | pdb_00005vdb

Crystal structure of a GNAT superfamily acetyltransferase PA4794 in complex with bisubstrate analog 3

spinqualitylabelsall models 5vdb, resolution 1.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vdb is a 1 chain structure with sequence from Pseae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 93M, SO4 Related: 4l8a, 5vd6 Gene: PA4794 (PSEAE) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Publication Abstract from PubMed Gcn5-related N-acetyltransferases (GNATs) are found in all kingdoms of life and catalyze important acyl transfer reactions in diverse cellular processes. While many 3D structures of GNATs have been determined, most do not contain acceptor substrates in their active sites. To expand upon existing crystallographic strategies for improving acceptor-bound GNAT structures, we synthesized peptide substrate analogs and reacted them with CoA in PA4794 protein crystals. We found two separate mechanisms for bisubstrate formation: (a) a novel X-ray induced radical-mediated alkylation of CoA with an alkene peptide and (b) direct alkylation of CoA with a halogenated peptide. Our approach is widely applicable across the GNAT superfamily and can be used to improve the success rate of obtaining liganded structures of other acyltransferases. Generating enzyme and radical-mediated bisubstrates as tools for investigating Gcn5-related N-acetyltransferases.,Reidl C, Majorek KA, Dang J, Tran D, Jew K, Law M, Payne Y, Minor W, Becker DP, Kuhn ML FEBS Lett. 2017 Aug;591(15):2348-2361. doi: 10.1002/1873-3468.12753. Epub 2017, Aug 1. PMID:28703494 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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