1GMU

Structure of UreE

Summary for 1GMU

• Entry DOI: 10.2210/pdb1gmu/pdb
• Related: 1GMV 1GMW
• Descriptor: UREE (2 entities in total)
• Functional Keywords: metallochaperone
• Biological source: KLEBSIELLA AEROGENES
• Cellular location: Cytoplasm: P18317
• Total number of polymer chains: 4
• Total formula weight: 62947.99

Authors

Song, H.K.,Mulrooney, S.B.,Huber, R.,Hausinger, R. (deposition date: 2001-09-24, release date: 2001-11-28, Last modification date: 2024-05-08)

Primary citation

Song, H.K.,Mulrooney, S.B.,Huber, R.,Hausinger, R.
Crystal Structure of Klebsiella Aerogenes Uree, a Nickel-Binding Metallochaperone for Urease Activation.
J.Biol.Chem., 276:49359-, 2001

PubMed Abstract: 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.

PubMed: 11591723
DOI: 10.1074/JBC.M108619200

Experimental method

X-RAY DIFFRACTION (1.5 Å)