Journal
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
Volume 17, Issue 5, Pages 787-797Publisher
TAYLOR & FRANCIS INC
DOI: 10.1080/07391102.2000.10506568
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A thorough conformational search of all the conformations available to oxygen-bound urea within wild-type urease was carried out. Identical low energy urea conformations were obtained by a Ramachandran type plot for the N-His272-Ni1-O-C-urea and Ni1-O-C-urea-N-urea dihedral angles. Ramachandran plots, with active sites and protonation states modified to model the different urease mechanisms, were used to evaluate the different mechanisms. Based upon the low energy conformations available to urea in the active site of wild-type urease one can conclude that the traditional His320 acts as a base mechanism is unlikely, while the N,O urea bridged and the reverse protonation mechanisms cannot be ruled out. A consensus hydrogen-bonding network that does not favor any of the mechanisms has been reconfirmed by the extensive conformational search.
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