1gmw

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Structure of UreE

Structural highlights

1gmw is a 4 chain structure with sequence from Klebsiella aerogenes. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.5Å
Ligands:CU, MSE
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

UREE_KLEAE Involved in urease metallocenter assembly. Binds about 6 nickel ions per homodimer. Probably functions as a nickel donor during metallocenter assembly. Its function can be bypassed in vitro in the presence of high nickel concentrations.[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

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
13 reviews cite this structure
Mulrooney et al. (2003)
No citations found

See Also

References

  1. Song HK, Mulrooney SB, Huber R, Hausinger RP. Crystal structure of Klebsiella aerogenes UreE, a nickel-binding metallochaperone for urease activation. J Biol Chem. 2001 Dec 28;276(52):49359-64. Epub 2001 Oct 8. PMID:11591723 doi:10.1074/jbc.M108619200

Contents


PDB ID 1gmw

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