4kr9 | pdb_00004kr9

Crystal structure of a 4-thiouridine synthetase - RNA complex at 3.5 Angstrom resolution

spinqualitylabelsall models 4kr9, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4kr9 is a 4 chain structure with sequence from Thema. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4kr6, 4kr7 Gene: AAD36761, thiI, TM_1694 (THEMA) Activity: tRNA sulfurtransferase, with EC number 2.8.1.4 Resources: FirstGlance, OCA, RCSB, PDBsum Function [THII_THEMA] Catalyzes the ATP-dependent transfer of a sulfur to tRNA to produce 4-thiouridine in position 8 of tRNAs, which functions as a near-UV photosensor. Also catalyzes the transfer of sulfur to the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. This is a step in the synthesis of thiazole, in the thiamine biosynthesis pathway. The sulfur is donated as persulfide by IscS (By similarity). Publication Abstract from PubMed In prokaryotes and archaea transfer ribonucleic acid (tRNA) stability as well as cellular UV protection relies on the post-transcriptional modification of uracil at position 8 (U8) of tRNAs by the 4-thiouridine synthetase ThiI. Here, we report three crystal structures of ThiI from Thermotoga maritima in complex with a truncated tRNA. The RNA is mainly bound by the N-terminal ferredoxin-like domain (NFLD) and the THUMP domain of one subunit within the ThiI homo-dimer thereby positioning the U8 close to the catalytic center in the pyrophosphatase domain of the other subunit. The recognition of the 3'-CCA end by the THUMP domain yields a molecular ruler defining the specificity for U8 thiolation. This first structure of a THUMP/NFLD-RNA complex might serve as paradigm for the RNA recognition by THUMP domains of other proteins. The ternary ThiI-RNA-ATP complex shows no significant structural changes due to adenosine triphosphate (ATP) binding, but two different states of active site loops are observed independent of the nucleotide loading state. Thereby conformational changes of the active site are coupled with conformational changes of the bound RNA. The ThiI-RNA complex structures indicate that full-length tRNA has to adopt a non-canonical conformation upon binding to ThiI. Crystal structure of a 4-thiouridine synthetase-RNA complex reveals specificity of tRNA U8 modification.,Neumann P, Lakomek K, Naumann PT, Erwin WM, Lauhon CT, Ficner R Nucleic Acids Res. 2014 Apr 5. PMID:24705700 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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