2bmi

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[[Image:2bmi.jpg|left|200px]]<br /><applet load="2bmi" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="2bmi, resolution 2.00&Aring;" />
 
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'''METALLO-BETA-LACTAMASE'''<br />
 
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==Overview==
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==METALLO-BETA-LACTAMASE==
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beta-Lactamases are extracellular or periplasmic bacterial enzymes which confer resistance to beta-lactam antibiotics. On the basis of their catalytic mechanisms, they can be divided into two major groups: active-site serine enzymes (classes A, C and D) and the ZnII enzymes (class B). The first crystal structure of a class B enzyme, the metallo-beta-lactamase from Bacillus cereus, has been solved at 2.5 A resolution [Carfi, Pares, Duee, Galleni, Duez, Frere &amp; Dideberg (1995). EMBO J. 14, 4914-4921]. Recently, the crystal structure of the metallo-beta-lactamase from Bacteroides fragilis has been determined in a tetragonal space group [Concha, Rasmussen, Bush &amp; Herzberg (1996). Structure, 4, 823-836]. The structure of the metallo-beta-lactamase from B. fragilis in an orthorhombic crystal form at 2.0 A resolution is reported here. The final crystallographic R is 0.196 for all the 32501 observed reflections in the range 10-2.0 A. The refined model includes 458 residues, 437 water molecules, four zinc and two sodium ions. These structures are discussed with reference to Zn binding and activity. A catalytic mechanism is proposed which is coherent with metallo-beta-lactamases being active with either one Zn ion (as in Aeromonas hydrophila) or two Zn ions (as in B. fragilis) bound to the protein.
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<StructureSection load='2bmi' size='340' side='right'caption='[[2bmi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2bmi]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1bmi 1bmi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BMI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BMI 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]] 2&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=2bmi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bmi OCA], [https://pdbe.org/2bmi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bmi RCSB], [https://www.ebi.ac.uk/pdbsum/2bmi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bmi ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/BLAB_BACFG BLAB_BACFG] Can hydrolyze carbapenem compounds.
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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/bm/2bmi_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=2bmi 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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2BMI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacteroides_fragilis Bacteroides fragilis] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=NA:'>NA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1BMI. 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=2BMI 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 structure of the ZnII beta-lactamase from Bacteroides fragilis in an orthorhombic crystal form., Carfi A, Duee E, Paul-Soto R, Galleni M, Frere JM, Dideberg O, Acta Crystallogr D Biol Crystallogr. 1998 Jan 1;54(Pt 1):45-57. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=9761816 9761816]
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[[Category: Bacteroides fragilis]]
[[Category: Bacteroides fragilis]]
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[[Category: Beta-lactamase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Carfi A]]
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[[Category: Carfi, A.]]
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[[Category: Dideberg O]]
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[[Category: Dideberg, O.]]
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[[Category: Duee E]]
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[[Category: Duee, E.]]
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[[Category: NA]]
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[[Category: ZN]]
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[[Category: beta-lactamase]]
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[[Category: metallo beta-lactamase]]
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[[Category: zinc]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:39:26 2008''
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Current revision

METALLO-BETA-LACTAMASE

PDB ID 2bmi

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