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1bue

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[[Image:1bue.jpg|left|200px]]<br /><applet load="1bue" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1bue, resolution 1.64&Aring;" />
 
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'''NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE'''<br />
 
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==Overview==
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==NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE==
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The treatment of infectious diseases by penicillin and cephalosporin antibiotics is continuously challenged by the emergence and the dissemination of the numerous TEM and SHV mutant beta-lactamases with extended substrate profiles. These class A beta-lactamases nevertheless remain inefficient against carbapenems, the most effective antibiotics against clinically relevant pathogens. A new member of this enzyme class, NMC-A, was recently reported to hydrolyze at high rates, and hence destroy, all known beta-lactam antibiotics, including carbapenems and cephamycins. The crystal structure of NMC-A was solved to 1.64-A resolution, and reveals modifications in the topology of the substrate-binding site. While preserving the geometry of the essential catalytic residues, the active site of the enzyme presents a disulfide bridge between residues 69 and 238, and certain other structural differences compared with the other beta-lactamases. These unusual features in class A beta-lactamases involve amino acids that participate in enzyme-substrate interactions, which suggested that these structural factors should be related to the very broad substrate specificity of this enzyme. The comparison of the NMC-A structure with those of other class A enzymes and enzyme-ligand complexes, indicated that the position of Asn-132 in NMC-A provides critical additional space in the region of the protein where the poorer substrates for class A beta-lactamases, such as cephamycins and carbapenems, need to be accommodated.
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<StructureSection load='1bue' size='340' side='right'caption='[[1bue]], [[Resolution|resolution]] 1.64&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1bue]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BUE FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.64&#8491;</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bue OCA], [https://pdbe.org/1bue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bue RCSB], [https://www.ebi.ac.uk/pdbsum/1bue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bue ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLAN_ENTCL BLAN_ENTCL] Hydrolyzes carbapenems such as imipenem, which are extended-spectrum beta-lactam antibiotics.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bu/1bue_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1bue ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1BUE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Enterobacter_cloacae Enterobacter cloacae]. 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=1BUE OCA].
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*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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X-ray analysis of the NMC-A beta-lactamase at 1.64-A resolution, a class A carbapenemase with broad substrate specificity., Swaren P, Maveyraud L, Raquet X, Cabantous S, Duez C, Pedelacq JD, Mariotte-Boyer S, Mourey L, Labia R, Nicolas-Chanoine MH, Nordmann P, Frere JM, Samama JP, J Biol Chem. 1998 Oct 9;273(41):26714-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9756914 9756914]
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[[Category: Beta-lactamase]]
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[[Category: Enterobacter cloacae]]
[[Category: Enterobacter cloacae]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Cabantous, S.]]
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[[Category: Cabantous S]]
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[[Category: Frere, J M.]]
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[[Category: Frere JM]]
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[[Category: Maveyraud, L.]]
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[[Category: Maveyraud L]]
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[[Category: Mourey, L.]]
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[[Category: Mourey L]]
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[[Category: Pedelacq, J D.]]
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[[Category: Pedelacq JD]]
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[[Category: Samama, J P.]]
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[[Category: Samama JP]]
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[[Category: Swaren, P.]]
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[[Category: Swaren P]]
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[[Category: antibiotic resistance]]
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[[Category: class a carbapenemase]]
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[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:16 2008''
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Current revision

NMC-A CARBAPENEMASE FROM ENTEROBACTER CLOACAE

PDB ID 1bue

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