4h1i | pdb_00004h1i

Structure of human thymidylate synthase at low salt conditions

spinqualitylabelsall models 4h1i, resolution 3.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4h1i is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: SO4 Related: 4gyh Gene: TYMS, TS, OK/SW-cl.29 (HUMAN) Activity: Thymidylate synthase, with EC number 2.1.1.45 Resources: FirstGlance, OCA, RCSB, PDBsum Function [TYSY_HUMAN] Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Publication Abstract from PubMed Expression of hTS (human thymidylate synthase), a key enzyme in thymidine biosynthesis, is regulated on the translational level through a feedback mechanism that is rarely found in eukaryotes. At low substrate concentrations, the ligand-free enzyme binds to its own mRNA and stabilizes a hairpin structure that sequesters the start codon. When in complex with dUMP (2'-deoxyuridine-5'-monophosphate) and a THF (tetrahydrofolate) cofactor, the enzyme adopts a conformation that is unable to bind and repress expression of mRNA. Here, we have used a combination of X-ray crystallography, RNA mutagenesis and site-specific cross-linking studies to investigate the molecular recognition of TS mRNA by the hTS enzyme. The interacting mRNA region was narrowed to the start codon and immediately flanking sequences. In the hTS enzyme, a helix-loop-helix domain on the protein surface was identified as the putative RNA-binding site. Analysis of mRNA recognition by human thymidylate synthase.,Brunn ND, Dibrov SM, Kao MB, Ghassemian M, Hermann T Biosci Rep. 2014 Dec 23;34(6). pii: e00168. doi: 10.1042/BSR20140137. PMID:25423174 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Thymidylate synthase

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