1EB0

Crystal structure of Bacillus pasteurii UreE at 1.85 A, phased by SIRAS. Type I crystal form.

Summary for 1EB0

• Entry DOI: 10.2210/pdb1eb0/pdb
• Related: 1EAR
• Descriptor: UREASE ACCESSORY PROTEIN UREE, ZINC ION (3 entities in total)
• Functional Keywords: chaperone, urease accessory protein, putative ni-chaperone
• Biological source: BACILLUS PASTEURII
• Total number of polymer chains: 1
• Total formula weight: 17478.34

Authors

Remaut, H.,Safarov, N.,Ciurli, S.,Van Beeumen, J. (deposition date: 2001-07-17, release date: 2002-01-04, Last modification date: 2024-05-08)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.85 Å)