2fu7

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[[Image:2fu7.jpg|left|200px]]
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{{Seed}}
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{{STRUCTURE_2fu7| PDB=2fu7 | SCENE= }}
{{STRUCTURE_2fu7| PDB=2fu7 | SCENE= }}
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'''Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (Cu-substituted form)'''
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===Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (Cu-substituted form)===
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 17999929 is the PubMed ID number.
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{{ABSTRACT_PUBMED_17999929}}
==About this Structure==
==About this Structure==
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==Reference==
==Reference==
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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]
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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]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 04:18:54 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 20:50:57 2008''

Revision as of 17:50, 2 July 2008

Image:2fu7.png

Template:STRUCTURE 2fu7

Zinc-beta-lactamase L1 from stenotrophomonas maltophilia (Cu-substituted form)

Template:ABSTRACT PUBMED 17999929

About this Structure

2FU7 is a Single protein structure of sequence from Stenotrophomonas maltophilia. Full crystallographic information is available from OCA.

Reference

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:17999929

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