1vio | pdb_00001vio

Crystal structure of pseudouridylate synthase

spinqualitylabelsall models 1vio, resolution 1.59Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1vio is a 2 chain structure with sequence from "bacterium_influenzae"_lehmann_and_neumann_1896 "bacterium influenzae" lehmann and neumann 1896. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BU1 Gene: RSUA, HI1243 ("Bacterium influenzae" Lehmann and Neumann 1896) Activity: Pseudouridylate synthase, with EC number 4.2.1.70 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RSUA_HAEIN] Responsible for synthesis of pseudouridine from uracil-516 in 16S ribosomal RNA (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed The structure of the pseudouridine synthase RsuA from Haemophilus influenza, which catalyzes the conversion of uridine to pseudouridine at a single position within 16S ribosomal RNA, has been determined at 1.59 A resolution and compared with that of Escherichia coli RsuA. The H. influenza enzyme contains an N-terminal S4-like alpha3beta4 domain followed by a catalytic domain, as observed in the structure of E. coli RsuA. Whereas the individual domains of E. coli and H. influenza RsuA are structurally similar, their relative spatial disposition differs greatly between the two structures. The former displays an extended open conformation with no direct contacts between the domains, while the latter is in a closed conformation with a large interface between the two domains. Domain closure presents several basic and polar residues into a putative RNA-binding cleft. It is proposed that this relative repositioning of the S4 and catalytic domains is used to modulate the shape and size of the rRNA-binding site in RsuA and in other pseudouridine synthases possessing S4 domains. Structure of the pseudouridine synthase RsuA from Haemophilus influenzae.,Matte A, Louie GV, Sivaraman J, Cygler M, Burley SK Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Apr 1;61(Pt, 4):350-4. Epub 2005 Mar 12. PMID:16511038 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also TRNA pseudouridine synthase

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