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New page: left|200px<br /><applet load="1m2x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m2x, resolution 1.5Å" /> '''Crystal Structure of ...
 
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[[Image:1m2x.jpg|left|200px]]<br /><applet load="1m2x" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1m2x, resolution 1.5&Aring;" />
'''Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril'''<br />


==Overview==
==Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril==
The crystal structure of the class-B beta-lactamase, BlaB, from the, pathogenic bacterium, Chryseobacterium meningosepticum, in complex with, the inhibitor, d-captopril, has been solved at 1.5-A resolution. The, enzyme has the typical alphabeta/betaalpha metallo-beta-lactamase fold and, the characteristic two metal binding sites of members of the subclass B1, in which two Zn2+ ions were identified. d-Captopril, a diastereoisomer of, the commercial drug, captopril, acts as an inhibitor by displacing the, catalytic hydroxyl ion required for antibiotic hydrolysis and, intercalating its sulfhydryl group between the two Zn2+ ions., Interestingly, d-captopril is located on one side of the active site, cleft. The x-ray structure of the complex of the closely related enzyme, IMP-1, with a mercaptocarboxylate inhibitor, which also contains a, sulfhydryl group bound to the two Zn2+ ions, shows the ligand to be, located on the opposite side of the active site cleft. A molecule, generated by fusion of these two inhibitors would cover the entire cleft, suggesting an interesting approach to the design of highly specific, inhibitors.
<StructureSection load='1m2x' size='340' side='right'caption='[[1m2x]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1m2x]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1M2X 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]] 1.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MCO:1-(3-MERCAPTO-2-METHYL-PROPIONYL)-PYRROLIDINE-2-CARBOXYLIC+ACID'>MCO</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=1m2x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m2x OCA], [https://pdbe.org/1m2x PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1m2x RCSB], [https://www.ebi.ac.uk/pdbsum/1m2x PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1m2x ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLAB1_ELIME BLAB1_ELIME] Hydrolyzes penicillins, cephalosporins (including cefoxitin), carbapenems and 6-beta-iodopenicillanate.
== 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/m2/1m2x_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1m2x ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1M2X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Elizabethkingia_meningoseptica Elizabethkingia meningoseptica] with NA, ZN, MCO and GOL 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M2X OCA].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The 1.5-A structure of Chryseobacterium meningosepticum zinc beta-lactamase in complex with the inhibitor, D-captopril., Garcia-Saez I, Hopkins J, Papamicael C, Franceschini N, Amicosante G, Rossolini GM, Galleni M, Frere JM, Dideberg O, J Biol Chem. 2003 Jun 27;278(26):23868-73. Epub 2003 Apr 8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12684522 12684522]
[[Category: Beta-lactamase]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Elizabethkingia meningoseptica]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Dideberg, O.]]
[[Category: Dideberg O]]
[[Category: Garcia-Saez, I.]]
[[Category: Garcia-Saez I]]
[[Category: GOL]]
[[Category: MCO]]
[[Category: NA]]
[[Category: ZN]]
[[Category: alpha-beta/beta-alpha fold.]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 21:06:16 2007''

Latest revision as of 07:39, 14 February 2024

Crystal Structure of the metallo-beta-lactamase BlaB of Chryseobacterium meningosepticum in complex with the inhibitor D-captopril

1m2x, resolution 1.50Å

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