1ear

Crystal structure of Bacillus pasteurii UreE at 1.7 A. Type II crystal form.

spinqualitylabelsall models 1ear, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1ear is a 1 chain structure with sequence from "urobacillus_pasteurii"_miquel_1889 "urobacillus pasteurii" miquel 1889. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ZN Related: 1eb0 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [UREE_BACPA] Involved in urease metallocenter assembly. Binds nickel. Probably functions as a nickel donor during metallocenter assembly.[HAMAP-Rule:MF_00822] 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 Bacillus pasteurii UreE (BpUreE) is a putative chaperone assisting the insertion of Ni(2+) ions in the active site of urease. The x-ray structure of the protein has been determined for two crystal forms, at 1.7 and 1.85 A resolution, using SIRAS phases derived from a Hg(2+)-derivative. BpUreE is composed of distinct N- and C-terminal domains, connected by a short flexible linker. The structure reveals the topology of an elongated homodimer, formed by interaction of the two C-terminal domains through hydrophobic interactions. A single Zn(2+) ion bound to four conserved His-100 residues, one from each monomer, connects two dimers resulting in a tetrameric BpUreE known to be formed in concentrated solutions. The Zn(2+) ion can be replaced by Ni(2+) as shown by anomalous difference maps obtained on a crystal of BpUreE soaked in a solution containing NiCl(2). A large hydrophobic patch surrounding the metal ion site is surface-exposed in the biologically relevant dimer. The BpUreE structure represents the first for this class of proteins and suggests a possible role for UreE in the urease nickel-center assembly. Structural basis for Ni(2+) transport and assembly of the urease active site by the metallochaperone UreE from Bacillus pasteurii.,Remaut H, Safarov N, Ciurli S, Van Beeumen J J Biol Chem. 2001 Dec 28;276(52):49365-70. Epub 2001 Oct 15. PMID:11602602 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Urease accessory protein

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