1ko3: Difference between revisions
No edit summary |
No edit summary |
||
Line 1: | Line 1: | ||
[[Image:1ko3.gif|left|200px]] | [[Image:1ko3.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1ko3", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1ko3| PDB=1ko3 | SCENE= }} | ||
}} | |||
'''VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced''' | '''VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced''' | ||
Line 30: | Line 27: | ||
[[Category: Garcia-Saez, I.]] | [[Category: Garcia-Saez, I.]] | ||
[[Category: Rossolini, G M.]] | [[Category: Rossolini, G M.]] | ||
[[Category: | [[Category: Alpha-beta/beta-alpha fold]] | ||
[[Category: | [[Category: Hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 22:58:13 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on |
Revision as of 22:58, 2 May 2008
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 Page seeded by OCA on Fri May 2 22:58:13 2008