1EAR

Crystal structure of Bacillus pasteurii UreE at 1.7 A. Type II crystal form.

1EAR の概要

• エントリーDOI: 10.2210/pdb1ear/pdb
• 関連するPDBエントリー: 1EB0
• 分子名称: UREASE ACCESSORY PROTEIN UREE, ZINC ION (3 entities in total)
• 機能のキーワード: chaperone, putative ni-chaperone, urease operon
• 由来する生物種: BACILLUS PASTEURII
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17478.34

構造登録者

Remaut, H.,Safarov, N.,Ciurli, S.,Van Beeumen, J. (登録日: 2001-07-16, 公開日: 2002-01-04, 最終更新日: 2023-12-13)

主引用文献

Reamut, H.,Safarov, N.,Ciurli, S.,Van Beeumen, J.
Structural Basis for Ni2+ Transport and Assembly of the Urease Active Site by the Metallochaperone Uree from Bacillus Pasteurii
J.Biol.Chem., 276:49365-, 2001

PubMed Abstract: 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 maps obtained on a crystal of BpUreE soaked in a solution containing NiCl(2). A large hydrophobic patch surrounding the metal ion site is surface-exposed in the biologically relevant dimer. The BpUreE structure represents the first for this class of proteins and suggests a possible role for UreE in the urease nickel-center assembly.

PubMed: 11602602
DOI: 10.1074/JBC.M108304200

実験手法

X-RAY DIFFRACTION (1.7 Å)