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The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution

The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å...  The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å resolution, 99.5% completeness, data redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the active site are separated by a distance of 3.53 Å. The structure clearly shows the binding mode of the inhibitor anion, symmetrically bridging the two Ni ions in the active site through the hydroxamate oxygen and chelating one Ni ion through the carbonyl oxygen. The flexible flap flanking the active site cavity is in the open conformation. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png JBIC Journal of Biological Inorganic Chemistry Springer Journals

The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 Å resolution

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Publisher
Springer Journals
Copyright
Copyright © 2000 by Society of Biological Inorganic Chemistry
Subject
Legacy
ISSN
0949-8257
eISSN
1432-1327
DOI
10.1007/s007750050014
Publisher site
See Article on Publisher Site

Abstract

 The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Å resolution, 99.5% completeness, data redundancy = 26, R-factor = 15.1%, PDB code 4UBP). The two Ni ions in the active site are separated by a distance of 3.53 Å. The structure clearly shows the binding mode of the inhibitor anion, symmetrically bridging the two Ni ions in the active site through the hydroxamate oxygen and chelating one Ni ion through the carbonyl oxygen. The flexible flap flanking the active site cavity is in the open conformation. The possible implications of the results on structure-based molecular design of new urease inhibitors are discussed.

Journal

JBIC Journal of Biological Inorganic ChemistrySpringer Journals

Published: Feb 22, 2000

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