1bmc: Difference between revisions

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New page: left|200px<br /> <applet load="1bmc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bmc, resolution 2.5Å" /> '''STRUCTURE OF A ZINC ...
 
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[[Image:1bmc.gif|left|200px]]<br />
<applet load="1bmc" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1bmc, resolution 2.5&Aring;" />
'''STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS'''<br />


==Overview==
==STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS==
The 3-D structure of Bacillus cereus (569/H/9) beta-lactamase (EC, 3.5.2.6), which catalyses the hydrolysis of nearly all beta-lactams, has, been solved at 2.5 A resolution by the multiple isomorphous replacement, method, with density modification and phase combination, from crystals of, the native protein and of a specially designed mutant (T97C). The current, model includes 212 of the 227 amino acid residues, the zinc ion and 10, water molecules. The protein is folded into a beta beta sandwich with, helices on each external face. To our knowledge, this fold has never been, observed. An approximate internal molecular symmetry is found, with a, 2-fold axis passing roughly through the zinc ion and suggesting a possible, gene duplication. The active site is located at one edge of the beta ... [[http://ispc.weizmann.ac.il/pmbin/getpm?7588620 (full description)]]
<StructureSection load='1bmc' size='340' side='right'caption='[[1bmc]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1bmc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BMC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BMC 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]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=1bmc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bmc OCA], [https://pdbe.org/1bmc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bmc RCSB], [https://www.ebi.ac.uk/pdbsum/1bmc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bmc ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLA2_BACCE BLA2_BACCE] 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/1bmc_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=1bmc ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1BMC is a [[http://en.wikipedia.org/wiki/Single_protein Single protein]] structure of sequence from [[http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]] with ZN as [[http://en.wikipedia.org/wiki/ligand ligand]]. Active as [[http://en.wikipedia.org/wiki/ ]], 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=1BMC OCA]].
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
 
__TOC__
==Reference==
</StructureSection>
The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold., Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O, EMBO J. 1995 Oct 16;14(20):4914-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7588620 7588620]
[[Category: Bacillus cereus]]
[[Category: Bacillus cereus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Carfi, A.]]
[[Category: Carfi A]]
[[Category: Dideberg, O.]]
[[Category: Dideberg O]]
[[Category: Duee, E.]]
[[Category: Duee E]]
[[Category: Pares, S.]]
[[Category: Pares S]]
[[Category: ZN]]
[[Category: antibiotic resistance]]
[[Category: hydrolase (acting in cyclic amides)]]
[[Category: signal]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Oct 29 18:48:53 2007''

Latest revision as of 06:37, 7 February 2024

STRUCTURE OF A ZINC METALLO-BETA-LACTAMASE FROM BACILLUS CEREUS

1bmc, resolution 2.50Å

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