1eb0
From Proteopedia
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[[Category: urease accessory protein]] | [[Category: urease accessory protein]] | ||
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Revision as of 13:05, 30 October 2007
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CRYSTAL STRUCTURE OF BACILLUS PASTEURII UREE AT 1.85 A, PHASED BY SIRAS. TYPE I CRYSTAL FORM.
Overview
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 ... [(full description)]
About this Structure
1EB0 is a [Single protein] structure of sequence from [Sporosarcina pasteurii] with ZN as [ligand]. Structure known Active Site: ZN. Full crystallographic information is available from [OCA].
Reference
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
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