2uyx
From Proteopedia
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[[Category: zinc]] | [[Category: zinc]] | ||
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Revision as of 15:36, 30 October 2007
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METALLO-BETA-LACTAMASE (1BC2) SINGLE POINT MUTANT D120S
Overview
Metallo-beta-lactamases are zinc-dependent hydrolases that inactivate, beta-lactam antibiotics, rendering bacteria resistant to them. Asp-120 is, fully conserved in all metallo-beta-lactamases and is central to, catalysis. Several roles have been proposed for Asp-120, but so far there, is no agreed consensus. We generated four site-specifically substituted, variants of the enzyme BcII from Bacillus cereus as follows: D120N, D120E, D120Q, and D120S. Replacement of Asp-120 by other residues with very, different metal ligating capabilities severely impairs the lactamase, activity without abolishing metal binding to the mutated site. A kinetic, study of these mutants indicates that Asp-120 is not the proton donor, nor, does it play an essential role in nucleophilic activation. Spectroscopic, ... [(full description)]
About this Structure
2UYX is a [Single protein] structure of sequence from [Bacillus cereus] with ZN and GOL as [ligands]. Active as [Beta-lactamase], with EC number [3.5.2.6]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].
Reference
Asp-120 locates Zn2 for optimal metallo-beta-lactamase activity., Llarrull LI, Fabiane SM, Kowalski JM, Bennett B, Sutton BJ, Vila AJ, J Biol Chem. 2007 Jun 22;282(25):18276-85. Epub 2007 Apr 10. PMID:17426028
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