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1gmu
From Proteopedia
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STRUCTURE OF UREE
Overview
UreE is proposed to be a metallochaperone that delivers nickel ions to, urease during activation of this bacterial virulence factor. Wild-type, Klebsiella aerogenes UreE binds approximately six nickel ions per, homodimer, whereas H144*UreE (a functional C-terminal truncated variant), was previously reported to bind two. We determined the structure of, H144*UreE by multi-wavelength anomalous diffraction and refined it to 1.5, A resolution. The present structure reveals an Hsp40-like peptide-binding, domain, an Atx1-like metal-binding domain, and a flexible C terminus., Three metal-binding sites per dimer, defined by structural analysis of, Cu-H144*UreE, are on the opposite face of the Atx1-like domain than, observed in the copper metallochaperone. One metal bridges the two, subunits via the pair of His-96 residues, whereas the other two sites, involve metal coordination by His-110 and His-112 within each subunit. In, contrast to the copper metallochaperone mechanism involving thiol ligand, exchanges between structurally similar chaperones and target proteins, we, propose that the Hsp40-like module interacts with urease apoprotein and/or, other urease accessory proteins, while the Atx1-like domain delivers, histidyl-bound nickel to the urease active site.
About this Structure
1GMU is a Single protein structure of sequence from Klebsiella aerogenes. Full crystallographic information is available from OCA.
Reference
Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation., Song HK, Mulrooney SB, Huber R, Hausinger RP, J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:11591723
Page seeded by OCA on Tue Nov 20 16:10:34 2007
