1GMU

Structure of UreE

1GMU の概要

• エントリーDOI: 10.2210/pdb1gmu/pdb
• 関連するPDBエントリー: 1GMV 1GMW
• 分子名称: UREE (2 entities in total)
• 機能のキーワード: metallochaperone
• 由来する生物種: KLEBSIELLA AEROGENES
• 細胞内の位置: Cytoplasm: P18317
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62947.99

構造登録者

Song, H.K.,Mulrooney, S.B.,Huber, R.,Hausinger, R. (登録日: 2001-09-24, 公開日: 2001-11-28, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (1.5 Å)