2fu6: Difference between revisions

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[[Image:2fu6.jpg|left|200px]]
{{Seed}}
[[Image:2fu6.png|left|200px]]


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{{STRUCTURE_2fu6|  PDB=2fu6  |  SCENE=  }}  
{{STRUCTURE_2fu6|  PDB=2fu6  |  SCENE=  }}  


'''Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form)'''
===Zinc-beta-lactamase l1 from stenotrophomonas maltophilia (apo form)===


==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 [[Single protein]] structure of sequence 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].  
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==
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]
<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 Sun May  4 04:18:48 2008''
 
''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

File:2fu6.png

Template:STRUCTURE 2fu6

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

  1. 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
  2. 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:https://dx.doi.org/10.1016/j.jmb.2004.10.070

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