4y4n | pdb_00004y4n

Thiazole synthase Thi4 from Methanococcus igneus

spinqualitylabelsall models 4y4n, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4y4n is a 8 chain structure with sequence from Methanotorris igneus Kol 5. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: 48H, FE2 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THI4_METIK Involved in the biosynthesis of the thiazole moiety of thiamine. Catalyzes the conversion of NAD and glycine to adenosine diphosphate 5-(2-hydroxyethyl)-4-methylthiazole-2-carboxylate (ADT), an adenylated thiazole intermediate, using free sulfide as a source of sulfur.[HAMAP-Rule:MF_00304] Publication Abstract from PubMed Thiamin diphosphate is an essential cofactor in all forms of life and plays a key role in amino acid and carbohydrate metabolism. Its biosynthesis involves separate syntheses of the pyrimidine and thiazole moieties, which are then coupled to form thiamin monophosphate. A final phosphorylation produces the active form of the cofactor. In most bacteria, six gene products are required for biosynthesis of the thiamin thiazole. In yeast and fungi only one gene product, Thi4, is required for thiazole biosynthesis. Methanococcus jannaschii expresses a putative Thi4 ortholog that was previously reported to be a ribulose 1, 5-bisphosphate synthase [Finn, M. W. and Tabita, F. R. (2004) J. Bacteriol. 186, 6360-6366]. Our structural studies show that the Thi4 orthologs from M. jannaschii and Methanococcus igneus are structurally homologous to Thi4 from Saccharomyces cerevisiae . In addition, all active site residues are conserved except for a key cysteine residue, which in S. cerevisiae is the source of the thiazole sulfur atom. Our recent biochemical studies showed that the archael Thi4 orthologs use nicotinamide adenine dinucleotide, glycine and free sulfide to form the thiamin thiazole in an iron-dependent reaction [Eser, B., Zhang, X., Chanani, P. K., Ealick, S.E., and Begley, T.P. (2015) submitted]. Here we report X-ray crystal structures of Thi4 from M. jannaschii complexed with ADP-ribulose, the C205S variant of Thi4 from S. cerevisiae with a bound glycine imine intermediate, and Thi4 from M. igneus with bound glycine imine intermediate and iron. These studies reveal the structural basis for the iron-dependent mechanism of sulfur transfer in archael and yeast thiazole synthases. Structural Basis for Iron-mediated Sulfur Transfer in Archael and Yeast Thiazole Synthases.,Zhang X, Eser BE, Chanani PK, Begley TP, Ealick SE Biochemistry. 2016 Feb 26. PMID:26919468 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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