1ko3: Difference between revisions

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|PDB= 1ko3 |SIZE=350|CAPTION= <scene name='initialview01'>1ko3</scene>, resolution 1.91&Aring;
|PDB= 1ko3 |SIZE=350|CAPTION= <scene name='initialview01'>1ko3</scene>, resolution 1.91&Aring;
|SITE=  
|SITE=  
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=OH:HYDROXIDE ION'>OH</scene>
|LIGAND= <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=OH:HYDROXIDE+ION'>OH</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY= [http://en.wikipedia.org/wiki/Hydrolase Hydrolase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.2.6 3.5.2.6]  
|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= blaVIM-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
|GENE= blaVIM-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=287 Pseudomonas aeruginosa])
|DOMAIN=
|RELATEDENTRY=[[1ko2|1KO2]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ko3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ko3 OCA], [http://www.ebi.ac.uk/pdbsum/1ko3 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ko3 RCSB]</span>
}}
}}


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==Reference==
==Reference==
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form., Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O, J Mol Biol. 2008 Jan 18;375(3):604-11. Epub 2007 Nov 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18061205 18061205]
The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form., Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O, J Mol Biol. 2008 Jan 18;375(3):604-11. Epub 2007 Nov 13. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18061205 18061205]
[[Category: Hydrolase]]
[[Category: Beta-lactamase]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Pseudomonas aeruginosa]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Garcia-Saez, I.]]
[[Category: Garcia-Saez, I.]]
[[Category: Rossolini, G M.]]
[[Category: Rossolini, G M.]]
[[Category: ACT]]
[[Category: CL]]
[[Category: OH]]
[[Category: ZN]]
[[Category: alpha-beta/beta-alpha fold]]
[[Category: alpha-beta/beta-alpha fold]]
[[Category: hydrolase]]
[[Category: hydrolase]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:19:58 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:51:12 2008''

Revision as of 21:51, 30 March 2008

File:1ko3.gif


PDB ID 1ko3

Drag the structure with the mouse to rotate
, resolution 1.91Å
Ligands: , , ,
Gene: blaVIM-2 (Pseudomonas aeruginosa)
Activity: Beta-lactamase, with EC number 3.5.2.6
Related: 1KO2


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



VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced


OverviewOverview

The crystal structures of the universally widespread metallo-beta-lactamase (MBL) Verona integron-encoded MBL (VIM)-2 from Pseudomonas aeruginosa have been solved in their native form as well as in an unexpected oxidised form. This carbapenem-hydrolysing enzyme belongs to the so-called B1 subfamily of MBLs and shares the folding of alpha beta/beta alpha sandwich, consisting of a core of beta-sheet surrounded by alpha-helices. Surprisingly, it showed a high tendency to be strongly oxidised at the catalytic cysteine located in the Cys site, Cys221, which, in the oxidised structure, becomes a cysteinesulfonic residue. Its native structure was obtained only in the presence of Tris(2-carboxyethyl)phosphine. This oxidation might be a consequence of a lower affinity for the second Zn located in the Cys site that would also explain the observed susceptibility of VIM-2 to chelating agents. This modification, if present in nature, might play a role in catalytic down-regulation. Comparison between native and oxidised VIM-2 and a predicted model of VIM-1 (which shows one residue different in the Cys site compared with VIM-2) is performed to explain the different activities and antibiotic specificities.

About this StructureAbout this Structure

1KO3 is a Single protein structure of sequence from Pseudomonas aeruginosa. Full crystallographic information is available from OCA.

ReferenceReference

The three-dimensional structure of VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa in its reduced and oxidised form., Garcia-Saez I, Docquier JD, Rossolini GM, Dideberg O, J Mol Biol. 2008 Jan 18;375(3):604-11. Epub 2007 Nov 13. PMID:18061205

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