1ko3
From Proteopedia
(New page: 200px<br /><applet load="1ko3" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ko3, resolution 1.91Å" /> '''VIM-2, a Zn-beta-lac...) |
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| - | [[Image:1ko3.gif|left|200px]]<br /><applet load="1ko3" size=" | + | [[Image:1ko3.gif|left|200px]]<br /><applet load="1ko3" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ko3, resolution 1.91Å" /> | caption="1ko3, resolution 1.91Å" /> | ||
'''VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced'''<br /> | '''VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced'''<br /> | ||
| + | |||
| + | ==Overview== | ||
| + | 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 Structure== | ==About this Structure== | ||
| - | 1KO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with ZN, ACT, CL and OH as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/ | + | 1KO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pseudomonas_aeruginosa Pseudomonas aeruginosa] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=OH:'>OH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KO3 OCA]. |
| - | [[Category: | + | |
| + | ==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://ispc.weizmann.ac.il//pmbin/getpm?pmid=18061205 18061205] | ||
| + | [[Category: Hydrolase]] | ||
[[Category: Pseudomonas aeruginosa]] | [[Category: Pseudomonas aeruginosa]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: ZN]] | [[Category: ZN]] | ||
[[Category: alpha-beta/beta-alpha fold]] | [[Category: alpha-beta/beta-alpha fold]] | ||
| + | [[Category: hydrolase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:01:18 2008'' |
Revision as of 09:01, 23 January 2008
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VIM-2, a Zn-beta-lactamase from Pseudomonas aeruginosa with Cys221 reduced
Overview
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 Structure
1KO3 is a Single protein structure of sequence from Pseudomonas aeruginosa with , , and as ligands. Active as Hydrolase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
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:18061205
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