4h67

Crystal structure of HMP synthase Thi5 from S. cerevisiae

spinqualitylabelsall models 4h67, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h67 is a 8 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.7Å Ligands: PLP, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function THI5_YEAST Proposed biosynthetic enzyme involved in pyrimidine biosynthesis pathway above the hydroxymethyl-pyrimidine precursor leading to the thiamine moiety. Publication Abstract from PubMed Vitamin B1 is essential for all organisms being well recognized as a necessary cofactor for key metabolic pathways such as glycolysis and was more recently implicated in DNA damage responses. Little is known about the enzyme responsible for the formation of the pyrimidine moiety (HMP-P synthase). We report a structure-function study of the HMP-P synthase from yeast, THI5p. Our crystallographic structure shows that the THI5p is a mix between periplasmic binding proteins and pyridoxal 5'-phosphate (PLP) dependent enzymes. Mutational and yeast complementation studies identify the key residues for HMP-P biosynthesis and offers unprecedented insights into the use of PLP as a substrate rather than as a cofactor, the requirement of iron and more generally into the HMP-P synthase reaction mechanism. The last piece in the vitamin B1 biosynthesis puzzle: Structural and functional insight into yeast HMP-P synthase.,Coquille S, Roux C, Fitzpatrick TB, Thore S J Biol Chem. 2012 Oct 9. PMID:23048037 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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