5n9x

Structure of adenylation domain THR1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces SP.OH-5093, ligand bound structure

spinqualitylabelsall models 5n9x, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5n9x is a 2 chain structure with sequence from Streptomyces sp.. This structure supersedes the now removed PDB entry 5apb. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.396Å Ligands: 8QN, ATP, MG, THR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function H6SG27_STRSQ Publication Abstract from PubMed We determined the crystal structure of Thr1, the self-standing adenylation domain involved in the nonribosomal-like biosynthesis of free 4-chlorothreonine in Streptomyces sp. OH-5093. Thr1 shows two monomers in the crystallographic asymmetric unit with different relative orientations of the C- and N-terminal subdomains both in the presence of substrates and in the unliganded form. Cocrystallization with substrates, adenosine 5'-triphosphate and l-threonine, yielded one monomer containing the two substrates and the other in complex with l-threonine adenylate, locked in a postadenylation state. Steady-state kinetics showed that Thr1 activates l-Thr and its stereoisomers, as well as d-Ala, l- and d-Ser, albeit with lower efficiency. Modeling of these substrates in the active site highlighted the molecular bases of substrate discrimination. This work provides the first crystal structure of a threonine-activating adenylation enzyme, a contribution to the studies on conformational rearrangement in adenylation domains and on substrate recognition in nonribosomal biosynthesis. DATABASE: Structural data are available in the Protein Data Bank under the accession number 5N9W and 5N9X. Structure of the adenylation domain Thr1 involved in the biosynthesis of 4-chlorothreonine in Streptomyces sp. OH-5093-protein flexibility and molecular bases of substrate specificity.,Scaglione A, Fullone MR, Montemiglio LC, Parisi G, Zamparelli C, Vallone B, Savino C, Grgurina I FEBS J. 2017 Sep;284(18):2981-2999. doi: 10.1111/febs.14163. Epub 2017 Aug 7. PMID:28704585 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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