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2fu6
From Proteopedia
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{{STRUCTURE_2fu6| PDB=2fu6 | SCENE= }} | {{STRUCTURE_2fu6| PDB=2fu6 | SCENE= }} | ||
| - | + | ===Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form)=== | |
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| - | ==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 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 Structure== | ==About this Structure== | ||
| - | 2FU6 is a | + | 2FU6 is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FU6 OCA]. |
==Reference== | ==Reference== | ||
| - | + | <ref group="xtra">PMID:7588620</ref><ref group="xtra">PMID:15588826</ref><references group="xtra"/> | |
[[Category: Beta-lactamase]] | [[Category: Beta-lactamase]] | ||
| - | [[Category: Single protein]] | ||
[[Category: Stenotrophomonas maltophilia]] | [[Category: Stenotrophomonas maltophilia]] | ||
[[Category: Dideberg, O.]] | [[Category: Dideberg, O.]] | ||
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[[Category: Metallo]] | [[Category: Metallo]] | ||
[[Category: Zn]] | [[Category: Zn]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
| + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 18:28:15 2009'' | ||
Revision as of 16:28, 16 February 2009
Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form)
About this Structure
2FU6 is a 2 chains structure of sequences from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.
Reference
- Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O. The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. EMBO J. 1995 Oct 16;14(20):4914-21. PMID:7588620
- Garau G, Bebrone C, Anne C, Galleni M, Frere JM, Dideberg O. A metallo-beta-lactamase enzyme in action: crystal structures of the monozinc carbapenemase CphA and its complex with biapenem. J Mol Biol. 2005 Jan 28;345(4):785-95. PMID:15588826 doi:http://dx.doi.org/10.1016/j.jmb.2004.10.070
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