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New page: left|200px<br /><applet load="1pio" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pio, resolution 2.8Å" /> '''AN ENGINEERED STAPHYL...
 
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[[Image:1pio.jpg|left|200px]]<br /><applet load="1pio" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1pio, resolution 2.8&Aring;" />
'''AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS'''<br />


==Overview==
==AN ENGINEERED STAPHYLOCOCCUS AUREUS PC1 BETA-LACTAMASE THAT HYDROLYSES THIRD GENERATION CEPHALOSPORINS==
The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an, Escherichia coli vector for site-directed mutagenesis and high-level, protein expression. A mutant enzyme has been produced in which Ala238 is, replaced by a serine, and Ile239 is deleted (A238S:I239del). The, engineered enzyme hydrolyses third-generation cephalosporins substantially, more rapidly than the parental enzyme does, while hydrolysis of, benzylpenicillin is slower with the mutant than with the wild-type and, native enzymes. The mutant beta-lactamase has been crystallized and the, structure determined and refined at 2.8 A resolution. The disposition of, the beta-strand which forms the side of the active site is altered in, comparison with the native S. aureus beta-lactamase structure, widening, the active site cleft and providing space to accommodate the bulky, side-chains of the third-generation cephalosporins.
<StructureSection load='1pio' size='340' side='right'caption='[[1pio]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1pio]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PIO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PIO 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]] 2.8&#8491;</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=1pio FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pio OCA], [https://pdbe.org/1pio PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pio RCSB], [https://www.ebi.ac.uk/pdbsum/1pio PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pio ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BLAC_STAAU BLAC_STAAU]
== 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/pi/1pio_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=1pio ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The beta-lactamase from Staphylococcus aureus PC1 has been cloned into an Escherichia coli vector for site-directed mutagenesis and high-level protein expression. A mutant enzyme has been produced in which Ala238 is replaced by a serine, and Ile239 is deleted (A238S:I239del). The engineered enzyme hydrolyses third-generation cephalosporins substantially more rapidly than the parental enzyme does, while hydrolysis of benzylpenicillin is slower with the mutant than with the wild-type and native enzymes. The mutant beta-lactamase has been crystallized and the structure determined and refined at 2.8 A resolution. The disposition of the beta-strand which forms the side of the active site is altered in comparison with the native S. aureus beta-lactamase structure, widening the active site cleft and providing space to accommodate the bulky side-chains of the third-generation cephalosporins.


==About this Structure==
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins.,Zawadzke LE, Smith TJ, Herzberg O Protein Eng. 1995 Dec;8(12):1275-85. PMID:8869640<ref>PMID:8869640</ref>
1PIO is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Staphylococcus_aureus Staphylococcus aureus]. 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=1PIO OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
An engineered Staphylococcus aureus PC1 beta-lactamase that hydrolyses third-generation cephalosporins., Zawadzke LE, Smith TJ, Herzberg O, Protein Eng. 1995 Dec;8(12):1275-85. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8869640 8869640]
</div>
[[Category: Beta-lactamase]]
<div class="pdbe-citations 1pio" style="background-color:#fffaf0;"></div>
[[Category: Single protein]]
 
==See Also==
*[[Beta-lactamase 3D structures|Beta-lactamase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Staphylococcus aureus]]
[[Category: Staphylococcus aureus]]
[[Category: Herzberg, O.]]
[[Category: Herzberg O]]
[[Category: Zawadzke, L.E.]]
[[Category: Zawadzke LE]]
[[Category: hydrolase (acting on cyclic amides)]]
 
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