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| [[Image:1bmc.gif|left|200px]] | | {{Seed}} |
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| {{STRUCTURE_1bmc| PDB=1bmc | SCENE= }} | | {{STRUCTURE_1bmc| PDB=1bmc | SCENE= }} |
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| '''STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''
| | ===STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS=== |
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| ==Overview==
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| 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. | | The line below this paragraph, {{ABSTRACT_PUBMED_7588620}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 7588620 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_7588620}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Antibiotic resistance]] | | [[Category: Antibiotic resistance]] |
| [[Category: Signal]] | | [[Category: Signal]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:41:52 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:22:45 2008'' |
