5upt | pdb_00005upt

Acyl-CoA synthetase PtmA2 from Streptomyces platensis in complex with SBNP468 ligand

spinqualitylabelsall models 5upt, resolution 1.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5upt is a 1 chain structure with sequence from Streptomyces platensis subsp. rosaceus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.92Å Ligands: 8JG, CL, GOL, MSE, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0A0V031_STRPT Publication Abstract from PubMed Acyl-coenzyme A (CoA) ligases catalyze the activation of carboxylic acids via a two-step reaction of adenylation followed by thioesterification. Here, we report the discovery of a non-adenylating acyl-CoA ligase PtmA2 and the functional separation of an acyl-CoA ligase reaction. Both PtmA1 and PtmA2, two acyl-CoA ligases from the biosynthetic pathway of platensimycin and platencin, are necessary for the two steps of CoA activation. Gene inactivation of ptmA1 and ptmA2 resulted in the accumulation of free acid and adenylate intermediates, respectively. Enzymatic and structural characterization of PtmA2 confirmed its ability to only catalyze thioesterification. Structural characterization of PtmA2 revealed it binds both free acid and adenylate substrates and undergoes the established mechanism of domain alternation. Finally, site-directed mutagenesis restored both the adenylation and complete CoA activation reactions. This study challenges the currently accepted paradigm of adenylating enzymes and inspires future investigations on functionally separated acyl-CoA ligases and their ramifications in biology. Natural separation of the acyl-CoA ligase reaction results in a non-adenylating enzyme.,Wang N, Rudolf JD, Dong LB, Osipiuk J, Hatzos-Skintges C, Endres M, Chang CY, Babnigg G, Joachimiak A, Phillips GN Jr, Shen B Nat Chem Biol. 2018 Jul;14(7):730-737. doi: 10.1038/s41589-018-0061-0. Epub 2018 , Jun 4. PMID:29867143 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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