1jea

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(New page: 200px<br /><applet load="1jea" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jea, resolution 2.0&Aring;" /> '''ALTERED TOPOLOGY AND ...)
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[[Image:1jea.jpg|left|200px]]<br /><applet load="1jea" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1jea, resolution 2.0&Aring;" />
 
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'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''<br />
 
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==Overview==
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==ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN==
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The three-dimensional structures of engineered variants of Bacillus lentus, subtilisin having increased enzymatic activity, K27R/N87S/V104Y/N123S/T274A (RSYSA) and N76D/N87S/S103A/V104I (DSAI), were, determined by X-ray crystallography. In addition to identifying changes in, atomic position we report a method that identifies protein segments having, altered flexibility. The method utilizes a statistical analysis of, variance to delineate main-chain temperature factors that represent, significant departures from the overall variance between equivalent, regions seen throughout the structure. This method reveals changes in, main-chain mobility in both variants. Residues 125-127 have increased, mobility in the RSYSA variant while residues 100-104 have decreased, mobility in the DSAI variant. These segments are located at the, substrate-binding site and changes in their mobility are believed to, relate to the observed changes in proteolytic activity. The effect of, altered crystal lattice contacts on segment flexibility becomes apparent, when identical variants, determined in two crystal forms, are compared, with the native enzyme.
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<StructureSection load='1jea' size='340' side='right'caption='[[1jea]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1jea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JEA FirstGlance]. <br>
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</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>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1jea FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jea OCA], [https://pdbe.org/1jea PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jea RCSB], [https://www.ebi.ac.uk/pdbsum/1jea PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jea ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/SUBS_LEDLE SUBS_LEDLE] Subtilisin is an extracellular alkaline serine protease, it catalyzes the hydrolysis of proteins and peptide amides.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/je/1jea_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=1jea ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1JEA is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Subtilisin Subtilisin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.62 3.4.21.62] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JEA OCA].
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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Engineered Bacillus lentus subtilisins having altered flexibility., Graycar T, Knapp M, Ganshaw G, Dauberman J, Bott R, J Mol Biol. 1999 Sep 10;292(1):97-109. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10493860 10493860]
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[[Category: Large Structures]]
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[[Category: Bacillus lentus]]
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[[Category: Lederbergia lenta]]
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[[Category: Single protein]]
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[[Category: Bott R]]
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[[Category: Subtilisin]]
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[[Category: Bott, R.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: calcium-binding]]
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[[Category: hydrolase]]
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[[Category: serine protease]]
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[[Category: sporulation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:09:34 2007''
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Current revision

ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN

PDB ID 1jea

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