2qdt

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[[Image:2qdt.jpg|left|200px]]<br /><applet load="2qdt" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2qdt.jpg|left|200px]]
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caption="2qdt, resolution 2.00&Aring;" />
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'''Structural Basis for the Broad-Spectrum Inhibition of Metallo-{Beta}-Lactamases: L1- IS38 Complex'''<br />
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{{Structure
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|PDB= 2qdt |SIZE=350|CAPTION= <scene name='initialview01'>2qdt</scene>, resolution 2.00&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=I38:N-(3-MERCAPTOPROPANOYL)-D-ALANINE'>I38</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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|GENE= L1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=40324 Stenotrophomonas maltophilia])
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}}
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'''Structural Basis for the Broad-Spectrum Inhibition of Metallo-{Beta}-Lactamases: L1- IS38 Complex'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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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].
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2QDT is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Stenotrophomonas_maltophilia Stenotrophomonas maltophilia]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2QDT OCA].
==Reference==
==Reference==
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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 Jun;51(6):2136-42. Epub 2007 Feb 16. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17307979 17307979]
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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 Jun;51(6):2136-42. Epub 2007 Feb 16. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17307979 17307979]
[[Category: Beta-lactamase]]
[[Category: Beta-lactamase]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zn]]
[[Category: zn]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:38:32 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 18:24:44 2008''

Revision as of 16:24, 20 March 2008

Image:2qdt.jpg


PDB ID 2qdt

Drag the structure with the mouse to rotate
, resolution 2.00Å
Ligands: , and
Gene: L1 (Stenotrophomonas maltophilia)
Activity: Beta-lactamase, with EC number 3.5.2.6
Coordinates: save as pdb, mmCIF, xml



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 nonrelated purposes. Pyridine carboxylates appear to be useful templates for the development of more-complex, selective, nontoxic inhibitors of subclass B2 metallo-beta-lactamases.

About this Structure

2QDT is a Single protein structure of sequence from Stenotrophomonas maltophilia. 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 Jun;51(6):2136-42. Epub 2007 Feb 16. PMID:17307979

Page seeded by OCA on Thu Mar 20 18:24:44 2008

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