1jea

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[[Image:1jea.jpg|left|200px]]
 
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==ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN==
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The line below this paragraph, containing "STRUCTURE_1jea", creates the "Structure Box" on the page.
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<StructureSection load='1jea' size='340' side='right'caption='[[1jea]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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or leave the SCENE parameter empty for the default display.
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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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{{STRUCTURE_1jea| PDB=1jea | SCENE= }}
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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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'''ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN'''
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==See Also==
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*[[Subtilisin 3D structures|Subtilisin 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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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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[[Category: Large Structures]]
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[[Category: Lederbergia lenta]]
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==About this Structure==
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[[Category: Bott R]]
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1JEA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_lentus Bacillus lentus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JEA OCA].
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==Reference==
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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://www.ncbi.nlm.nih.gov/pubmed/10493860 10493860]
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[[Category: Bacillus lentus]]
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[[Category: Single protein]]
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[[Category: Subtilisin]]
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[[Category: Bott, R.]]
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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://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:07:03 2008''
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Current revision

ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN

PDB ID 1jea

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