4xp7 | pdb_00004xp7

Crystal structure of Human tRNA dihydrouridine synthase 2

spinqualitylabelsall models 4xp7, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4xp7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: CSO, FNR Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function DUS2_HUMAN Regulates mitogenic signal transduction by dephosphorylating both Thr and Tyr residues on MAP kinases ERK1 and ERK2. Publication Abstract from PubMed The reduction of uridine to dihydrouridine at specific positions in tRNA is catalysed by dihydrouridine synthase (Dus) enzymes. Increased expression of human dihydrouridine synthase 2 (hDus2) has been linked to pulmonary carcinogenesis, while its knockdown decreased cancer cell line viability, suggesting that it may serve as a valuable target for therapeutic intervention. Here, the X-ray crystal structure of a construct of hDus2 encompassing the catalytic and tRNA-recognition domains (residues 1-340) determined at 1.9 A resolution is presented. It is shown that the structure can be determined automatically by phenix.mr_rosetta starting from a bacterial Dus enzyme with only 18% sequence identity and a significantly divergent structure. The overall fold of the human Dus2 is similar to that of bacterial enzymes, but has a larger recognition domain and a unique three-stranded antiparallel beta-sheet insertion into the catalytic domain that packs next to the recognition domain, contributing to domain-domain interactions. The structure may inform the development of novel therapeutic approaches in the fight against lung cancer. From bacterial to human dihydrouridine synthase: automated structure determination.,Whelan F, Jenkins HT, Griffiths SC, Byrne RT, Dodson EJ, Antson AA Acta Crystallogr D Biol Crystallogr. 2015 Jul 1;71(Pt 7):1564-71. doi:, 10.1107/S1399004715009220. Epub 2015 Jun 30. PMID:26143927 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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