2fu8
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Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (d-captopril complex)
OverviewOverview
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 beta, sandwich and near the N-terminal end of a helix. The zinc ion is, coordinated by three histidine residues (86, 88 and 149) and a water, molecule. A sequence comparison of the relevant metallo-beta-lactamases, based on this protein structure, highlights a few well-conserved amino, acid residues. The structure shows that most of these residues are in the, active site. Among these, aspartic acid 90 and histidine 210 participate, in a proposed catalytic mechanism for beta-lactam hydrolysis.
About this StructureAbout this Structure
2FU8 is a Single protein structure of sequence from Stenotrophomonas maltophilia with ZN, SO4, MCO and GOL as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
ReferenceReference
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
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