2bmi: Difference between revisions

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New page: left|200px<br /><applet load="2bmi" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bmi, resolution 2.00Å" /> '''METALLO-BETA-LACTAMA...
 
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[[Image:2bmi.jpg|left|200px]]<br /><applet load="2bmi" size="450" color="white" frame="true" align="right" spinBox="true"
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'''METALLO-BETA-LACTAMASE'''<br />


==Overview==
==METALLO-BETA-LACTAMASE==
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.
<StructureSection load='2bmi' size='340' side='right'caption='[[2bmi]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLAB_BACFG BLAB_BACFG] Can hydrolyze carbapenem compounds.
== 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/bm/2bmi_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=2bmi ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
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 ZN and NA as [http://en.wikipedia.org/wiki/ligands ligands]. This structure superseeds 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BMI OCA].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
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]
[[Category: Bacteroides fragilis]]
[[Category: Bacteroides fragilis]]
[[Category: Beta-lactamase]]
[[Category: Large Structures]]
[[Category: Single protein]]
[[Category: Carfi A]]
[[Category: Carfi, A.]]
[[Category: Dideberg O]]
[[Category: Dideberg, O.]]
[[Category: Duee E]]
[[Category: Duee, E.]]
[[Category: NA]]
[[Category: ZN]]
[[Category: beta-lactamase]]
[[Category: metallo beta-lactamase]]
[[Category: zinc]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:50:02 2007''

Latest revision as of 12:17, 14 February 2024

METALLO-BETA-LACTAMASEMETALLO-BETA-LACTAMASE

Structural highlights

2bmi is a 2 chain structure with sequence from Bacteroides fragilis. This structure supersedes the now removed PDB entry 1bmi. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BLAB_BACFG Can hydrolyze carbapenem compounds.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2bmi, resolution 2.00Å

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