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| {{STRUCTURE_2fu8| PDB=2fu8 | SCENE= }} | | {{STRUCTURE_2fu8| PDB=2fu8 | SCENE= }} |
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| '''Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (d-captopril complex)'''
| | ===Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (d-captopril complex)=== |
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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_17999929}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17999929 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17999929}} |
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| ==About this Structure== | | ==About this Structure== |
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| ==Reference== | | ==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:[http://www.ncbi.nlm.nih.gov/pubmed/7588620 7588620]
| | Structural insights into the design of inhibitors for the L1 metallo-beta-lactamase from Stenotrophomonas maltophilia., Nauton L, Kahn R, Garau G, Hernandez JF, Dideberg O, J Mol Biol. 2008 Jan 4;375(1):257-69. Epub 2007 Oct 22. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17999929 17999929] |
| [[Category: Beta-lactamase]] | | [[Category: Beta-lactamase]] |
| [[Category: Single protein]] | | [[Category: Single protein]] |
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| [[Category: Metallo]] | | [[Category: Metallo]] |
| [[Category: Zn]] | | [[Category: Zn]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:18:54 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:51:10 2008'' |