2p9v: Difference between revisions
New page: left|200px<br /><applet load="2p9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="2p9v, resolution 1.80Å" /> '''Structure of AmpC be... |
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[[Image:2p9v.jpg|left|200px]]<br /><applet load="2p9v" size=" | [[Image:2p9v.jpg|left|200px]]<br /><applet load="2p9v" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2p9v, resolution 1.80Å" /> | caption="2p9v, resolution 1.80Å" /> | ||
'''Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor'''<br /> | '''Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2P9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with PO4 as [http://en.wikipedia.org/wiki/ligand ligand]. 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:// | 2P9V is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=PO4:'>PO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2P9V OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 14:12:46 2008'' | ||
Revision as of 15:12, 23 January 2008
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Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor
OverviewOverview
O-Aryloxycarbonyl hydroxamates represent a new class of beta-lactamase, inhibitors. N-Benzyloxycarbonyl-O-(phenoxycarbonyl) hydroxylamine, for, example, inactivates the class C Enterobacter cloacae P99 beta-lactamase, with a rate constant of 6.1 x 103 s-1 M-1; approximately two turnover, events accompany the inhibition., N-Benzyloxycarbonyl-O-[(3-carboxyphenoxy)carbonyl] hydroxylamine is, comparably effective. These compounds also inactivate the class A TEM, beta-lactamase. A crystal structure of the inactivated AmpC enzyme, another class C beta-lactamase, reveals that the active site has become, cross-linked by a carbamate bridge spanning Ser64, the active site, nucleophile, and Lys315, a conserved active site residue.
About this StructureAbout this Structure
2P9V is a Protein complex structure of sequences from Escherichia coli with as ligand. Active as Beta-lactamase, with EC number 3.5.2.6 Full crystallographic information is available from OCA.
ReferenceReference
O-Aryloxycarbonyl Hydroxamates: New beta-Lactamase Inhibitors That Cross-Link the Active Site., Wyrembak PN, Babaoglu K, Pelto RB, Shoichet BK, Pratt RF, J Am Chem Soc. 2007 Aug 8;129(31):9548-9. Epub 2007 Jul 12. PMID:17628063
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