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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="450" color="white" frame="true" align="right" spinBox="true"
caption="2p9v, resolution 1.80&Aring;" />
'''Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor'''<br />


==Overview==
==Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor==
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.
<StructureSection load='2p9v' size='340' side='right'caption='[[2p9v]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2p9v]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P9V OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P9V FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=KCX:LYSINE+NZ-CARBOXYLIC+ACID'>KCX</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2p9v FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p9v OCA], [https://pdbe.org/2p9v PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p9v RCSB], [https://www.ebi.ac.uk/pdbsum/2p9v PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p9v ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/AMPC_ECOLI AMPC_ECOLI] This protein is a serine beta-lactamase with a substrate specificity for cephalosporins.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/p9/2p9v_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2p9v ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2P9V OCA].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17628063 17628063]
[[Category: Beta-lactamase]]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Protein complex]]
[[Category: Large Structures]]
[[Category: Babaoglu, K.]]
[[Category: Babaoglu K]]
[[Category: Pelto, R.B.]]
[[Category: Pelto RB]]
[[Category: Pratt, R.F.]]
[[Category: Pratt RF]]
[[Category: Shoichet, B.K.]]
[[Category: Shoichet BK]]
[[Category: Wyrembak, P.N.]]
[[Category: Wyrembak PN]]
[[Category: PO4]]
[[Category: beta-lactamase]]
[[Category: cross-link]]
[[Category: hydrolase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 13:28:29 2007''

Latest revision as of 22:27, 26 March 2025

Structure of AmpC beta-lactamase with cross-linked active site after exposure to small molecule inhibitor

2p9v, resolution 1.80Å

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