2qdt
From Proteopedia
(New page: 200px<br /><applet load="2qdt" size="450" color="white" frame="true" align="right" spinBox="true" caption="2qdt, resolution 2.00Å" /> '''Structural Basis for...) |
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| - | [[Image:2qdt.jpg|left|200px]]<br /><applet load="2qdt" size=" | + | [[Image:2qdt.jpg|left|200px]]<br /><applet load="2qdt" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2qdt, resolution 2.00Å" /> | caption="2qdt, resolution 2.00Å" /> | ||
'''Structural Basis for the Broad-Spectrum Inhibition of Metallo-{Beta}-Lactamases: L1- IS38 Complex'''<br /> | '''Structural Basis for the Broad-Spectrum Inhibition of Metallo-{Beta}-Lactamases: L1- IS38 Complex'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2QDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia] with ZN, SO4 and I38 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http:// | + | 2QDT is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia] with <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=I38:'>I38</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QDT OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zn]] | [[Category: zn]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:52:39 2008'' |
Revision as of 11:52, 23 January 2008
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Structural Basis for the Broad-Spectrum Inhibition of Metallo-{Beta}-Lactamases: L1- IS38 Complex
Overview
Various inhibitors of metallo-beta-lactamases have been reported, however, none are effective for all subgroups. Those that have been found to, inhibit the enzymes of subclass B2 (catalytically active with one zinc), either contain a thiol (and show less inhibition towards this subgroup, than towards the dizinc members of B1 and B3) or are inactivators behaving, as substrates for the dizinc family members. The present work reveals that, certain pyridine carboxylates are competitive inhibitors of CphA, a, subclass B2 enzyme. X-ray crystallographic analyses demonstrate that, pyridine-2,4-dicarboxylic acid chelates the zinc ion in a bidentate manner, within the active site. Salts of these compounds are already available and, undergoing biomedical testing for various non-related purposes., Pyridine-carboxylates appear useful templates for the development of more, complex, selective, non-toxic inhibitors of the subclass B2, metallo-beta-lactamases.
About this Structure
2QDT is a Single protein structure of sequence from Stenotrophomonas maltophilia with , and as ligands. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
Reference
Competitive Inhibitors of the CphA Metallo-{beta}-Lactamase from Aeromonas hydrophila., Horsfall LE, Garau G, Lienard BM, Dideberg O, Schofield CJ, Frere JM, Galleni M, Antimicrob Agents Chemother. 2007 Feb 16;. PMID:17307979
Page seeded by OCA on Wed Jan 23 13:52:39 2008
Categories: Beta-lactamase | Single protein | Stenotrophomonas maltophilia | Dideberg, O. | Garau, G. | I38 | SO4 | ZN | Hydrolase | Inhibitor | L1 | Lactamase | Metallo | Zn
