Abstract
The structure of β-mercaptoethanol-inhibited urease from Bacillus pasteurii, a highly ureolytic soil micro-organism, was solved at 1.65 Å using synchrotron X-ray cryogenic diffraction data. The structure clearly shows the unexpected binding mode of β-mercaptoethanol, which bridges the two nickel ions in the active site through the sulfur atom and chelates one Ni through the OH functionality. Another molecule of inhibitor forms a mixed disulfide with a Cys residue, thus sealing the entrance to the active site cavity by steric hindrance. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.
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Received: 31 December 1997 / Accepted: 25 February 1998
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Benini, S., Rypniewski, W., Wilson, K. et al. The complex of Bacillus pasteurii urease with β-mercaptoethanol from X-ray data at 1.65-Å resolution. JBIC 3, 268–273 (1998). https://doi.org/10.1007/s007750050231
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DOI: https://doi.org/10.1007/s007750050231