2fu7

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|PDB= 2fu7 |SIZE=350|CAPTION= <scene name='initialview01'>2fu7</scene>, resolution 1.85&Aring;
|PDB= 2fu7 |SIZE=350|CAPTION= <scene name='initialview01'>2fu7</scene>, resolution 1.85&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=PHN:1,10-PHENANTHROLINE'>PHN</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|LIGAND= <scene name='pdbligand=CU:COPPER+(II)+ION'>CU</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PHN:1,10-PHENANTHROLINE'>PHN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Beta-lactamase Beta-lactamase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6] </span>
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia])
|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia])
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|DOMAIN=
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|RELATEDENTRY=[[2fm6|2FM6]], [[2fu6|2FU6]], [[2fu8|2FU8]], [[2fu9|2FU9]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2fu7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2fu7 OCA], [http://www.ebi.ac.uk/pdbsum/2fu7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2fu7 RCSB]</span>
}}
}}
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[[Category: Kahn, R.]]
[[Category: Kahn, R.]]
[[Category: Nauton, L.]]
[[Category: Nauton, L.]]
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[[Category: CU]]
 
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[[Category: GOL]]
 
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[[Category: PHN]]
 
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[[Category: SO4]]
 
[[Category: beta]]
[[Category: beta]]
[[Category: hydrolase]]
[[Category: hydrolase]]
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[[Category: zn]]
[[Category: zn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:56:48 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 03:07:41 2008''

Revision as of 00:07, 31 March 2008

Image:2fu7.jpg


PDB ID 2fu7

Drag the structure with the mouse to rotate
, resolution 1.85Å
Ligands: , , ,
Gene: L1 (Stenotrophomonas maltophilia)
Activity: Beta-lactamase, with EC number 3.5.2.6
Related: 2FM6, 2FU6, 2FU8, 2FU9


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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

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:7588620

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