3bfg: Difference between revisions

New page: left|200px<br /><applet load="3bfg" size="350" color="white" frame="true" align="right" spinBox="true" caption="3bfg, resolution 2.0Å" /> '''class A beta-lactamas...
 
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'''class A beta-lactamase SED-G238C complexed with meropenem'''<br />


==Overview==
==class A beta-lactamase SED-G238C complexed with meropenem==
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type, extended-spectrum beta-lactamase that has the ability to hydrolyze, expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED, mutant in which Gly238 has been replaced by a cysteine, forming a, disulfide bridge with the other Cys residue located at position 69, (SED-G238C), have been crystallized. The crystals belong to the monoclinic, space group C2, with unit-cell parameters a = 188.09, b = 73.65, c =, 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c =, 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray, diffraction data were collected to maximum resolutions of 2.4 A for SED-1, and 2.0 A for SED-G238C.
<StructureSection load='3bfg' size='340' side='right'caption='[[3bfg]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3bfg]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Citrobacter_sedlakii Citrobacter sedlakii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3BFG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3BFG 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=MER:(4R,5S)-3-{[(3S,5S)-5-(DIMETHYLCARBAMOYL)PYRROLIDIN-3-YL]SULFANYL}-5-[(2S,3R)-3-HYDROXY-1-OXOBUTAN-2-YL]-4-METHYL-4,5-DIHYDRO-1H-PYRROLE-2-CARBOXYLIC+ACID'>MER</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=3bfg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bfg OCA], [https://pdbe.org/3bfg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3bfg RCSB], [https://www.ebi.ac.uk/pdbsum/3bfg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3bfg ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q93PQ0_9ENTR Q93PQ0_9ENTR]
== 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/bf/3bfg_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3bfg ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
SED-1, a class A beta-lactamase from Citrobacter sedlakii, is a CTX-M-type extended-spectrum beta-lactamase that has the ability to hydrolyze expanded-spectrum cephalosporins such as cefotaxime. SED-1 and a SED mutant in which Gly238 has been replaced by a cysteine, forming a disulfide bridge with the other Cys residue located at position 69 (SED-G238C), have been crystallized. The crystals belong to the monoclinic space group C2, with unit-cell parameters a = 188.09, b = 73.65, c = 105.41 A, beta = 121.67 degrees for SED-1 and a = 187.64, b = 73.2, c = 103.89 A, beta = 121.89 degrees for the SED-G238C mutant. X-ray diffraction data were collected to maximum resolutions of 2.4 A for SED-1 and 2.0 A for SED-G238C.


==About this Structure==
Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii.,Petrella S, Pernot L, Sougakoff W Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):125-8. Epub 2003, Dec 18. PMID:014684905<ref>PMID:014684905</ref>
3BFG is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Citrobacter_sedlakii Citrobacter sedlakii] with <scene name='pdbligand=MER:'>MER</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=3BFG OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Crystallization and preliminary X-ray diffraction study of the class A beta-lactamase SED-1 and its mutant SED-G238C from Citrobacter sedlakii., Petrella S, Pernot L, Sougakoff W, Acta Crystallogr D Biol Crystallogr. 2004 Jan;60(Pt 1):125-8. Epub 2003, Dec 18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14684905 14684905]
</div>
[[Category: Beta-lactamase]]
<div class="pdbe-citations 3bfg" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Citrobacter sedlakii]]
[[Category: Citrobacter sedlakii]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Pernot, L.]]
[[Category: Pernot L]]
[[Category: Petrella, S.]]
[[Category: Petrella S]]
[[Category: Sougakoff, W.]]
[[Category: Sougakoff W]]
[[Category: MER]]
[[Category: acyl-enzyme]]
[[Category: beta-lactamase]]
[[Category: class a]]
[[Category: hydrolase]]
[[Category: meropenem]]
[[Category: sed-g238c]]
 
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