1bmc
From Proteopedia
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STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS
Overview
The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC, 3.5.2.6), which catalyses the hydrolysis of nearly all beta-lactams, has, been solved at 2.5 A resolution by the multiple isomorphous replacement, method, with density modification and phase combination, from crystals of, the native protein and of a specially designed mutant (T97C). The current, model includes 212 of the 227 amino acid residues, the zinc ion and 10, water molecules. The protein is folded into a beta beta sandwich with, helices on each external face. To our knowledge, this fold has never been, observed. An approximate internal molecular symmetry is found, with a, 2-fold axis passing roughly through the zinc ion and suggesting a possible, gene duplication. The active site is located at one edge of the beta ... [(full description)]
About this Structure
1BMC is a [Single protein] structure of sequence from [Bacillus cereus] with ZN as [ligand]. Active as [[1]], with EC number [3.5.2.6]. Full crystallographic information is available from [OCA].
Reference
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:7588620
Page seeded by OCA on Mon Oct 29 18:48:53 2007
