Please use this identifier to cite or link to this item:
Title: The complex of Bacillus pasteurii urease with acetohydroxamate anion from X-ray data at 1.55 angstrom resolution
Authors: S., Benini
W. R., Rypniewski
K. S., Wilson
S., Miletti
S., Ciurli
Mangani, Stefano 
Keywords: X-ray; crystal structure; urease; inhibitor; mechanism
Issue Date: 2000
Project: None 
Journal: JBIC
The structure of Bacillus pasteurii urease inhibited with acetohydroxamic acid was solved and refined anisotropically using synchrotron X-ray cryogenic diffraction data (1.55 Angstrom resolution, 99.5% clompleteness, 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 Angstrom 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.
ISSN: 0949-8257
DOI: 10.1007/s007750050014
Appears in Collections:Publications

Show full item record

Google ScholarTM



Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.