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1p10

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STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES

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Retrieved from "http://52.214.119.220/wiki/index.php/1p10"

Categories: Large Structures | Lysobacter enzymogenes | Agard DA | Bone R

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-[[Image:1p10.gif|left|200px]]<br /><applet load="1p10" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1p10, resolution 2.25&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='1p10' size='340' side='right'caption='[[1p10]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1p10]] is a 2 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=1P10 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1P10 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]] 2.25&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B2V:VALINE+BORONIC+ACID'>B2V</scene>, <scene name='pdbligand=MSU:SUCCINIC+ACID+MONOMETHYL+ESTER'>MSU</scene>, <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=1p10 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1p10 OCA], [https://pdbe.org/1p10 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1p10 RCSB], [https://www.ebi.ac.uk/pdbsum/1p10 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1p10 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/p1/1p10_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=1p10 ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-P10 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=1P10 OCA].
+*[[Alpha-lytic protease 3D structures|Alpha-lytic protease 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-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]
+[[Category: Large Structures]]
-[[Category: Alpha-lytic endopeptidase]]
 [[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)]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:21:48 2007''

1p10

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STRUCTURAL PLASTICITY AS A DETERMINANT OF ENZYME SPECIFICITY. CREATING BROADLY SPECIFIC PROTEASES

Structural highlights

Function

Evolutionary Conservation

See Also

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