1p09: Difference between revisions

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New page: left|200px<br /><applet load="1p09" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p09, resolution 2.20Å" /> '''STRUCTURAL PLASTICIT...
 
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[[Image:1p09.gif|left|200px]]<br /><applet load="1p09" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1p09, resolution 2.20&Aring;" />
'''STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES'''<br />


==Overview==
==STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES==
The substrate specificity of alpha-lytic protease has been changed, dramatically, with a concomitant increase in activity, by replacing an, active-site Met with Ala. The substrate specificity of both this mutant, and another similar mutant are extraordinarily broad. X-ray, crystallographic analysis shows that structural plasticity, a combination, of alternate side-chain conformations and binding-site flexibility, allows, both large and small substrates to be well accommodated.
<StructureSection load='1p09' size='340' side='right'caption='[[1p09]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1p09]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1P09 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P09 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]] 2.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=1p09 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p09 OCA], [https://pdbe.org/1p09 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p09 RCSB], [https://www.ebi.ac.uk/pdbsum/1p09 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p09 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PRLA_LYSEN PRLA_LYSEN]
== 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/p0/1p09_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=1p09 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The substrate specificity of alpha-lytic protease has been changed dramatically, with a concomitant increase in activity, by replacing an active-site Met with Ala. The substrate specificity of both this mutant and another similar mutant are extraordinarily broad. X-ray crystallographic analysis shows that structural plasticity, a combination of alternate side-chain conformations and binding-site flexibility, allows both large and small substrates to be well accommodated.


==About this Structure==
Structural plasticity broadens the specificity of an engineered protease.,Bone R, Silen JL, Agard DA Nature. 1989 May 18;339(6221):191-5. PMID:2716847<ref>PMID:2716847</ref>
1P09 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lysobacter_enzymogenes Lysobacter enzymogenes] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Alpha-lytic_endopeptidase Alpha-lytic endopeptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.12 3.4.21.12] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1P09 OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Structural plasticity broadens the specificity of an engineered protease., Bone R, Silen JL, Agard DA, Nature. 1989 May 18;339(6221):191-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=2716847 2716847]
</div>
[[Category: Alpha-lytic endopeptidase]]
<div class="pdbe-citations 1p09" style="background-color:#fffaf0;"></div>
 
==See Also==
*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Lysobacter enzymogenes]]
[[Category: Lysobacter enzymogenes]]
[[Category: Single protein]]
[[Category: Agard DA]]
[[Category: Agard, D.A.]]
[[Category: Bone R]]
[[Category: Bone, R.]]
[[Category: SO4]]
[[Category: hydrolase (serine proteinase)]]
 
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Retrieved from "https://proteopedia.org/1p09"