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1iav

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[[Image:1iav.gif|left|200px]]<br /><applet load="1iav" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1iav, resolution 1.80&Aring;" />
 
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'''STRUCTURE ON NATIVE (ASN 87) SUBTILISIN FROM BACILLUS LENTUS'''<br />
 
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==Overview==
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==STRUCTURE ON NATIVE (ASN 87) SUBTILISIN FROM BACILLUS LENTUS==
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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='1iav' size='340' side='right'caption='[[1iav]], [[Resolution|resolution]] 1.80&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1iav]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lederbergia_lenta Lederbergia lenta]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1c13 1c13]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IAV 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]] 1.8&#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=SEB:O-BENZYLSULFONYL-SERINE'>SEB</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=1iav FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1iav OCA], [https://pdbe.org/1iav PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1iav RCSB], [https://www.ebi.ac.uk/pdbsum/1iav PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1iav 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/ia/1iav_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=1iav 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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1IAV 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 <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. This structure supersedes the now removed PDB entry 1C13. 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://oca.weizmann.ac.il/oca-bin/ocashort?id=1IAV 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: Knapp M]]
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[[Category: Bott, R.]]
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[[Category: Knapp, M.]]
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[[Category: CA]]
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[[Category: SO4]]
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[[Category: altered flexibility]]
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[[Category: subtilisins]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:09:51 2008''
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Current revision

STRUCTURE ON NATIVE (ASN 87) SUBTILISIN FROM BACILLUS LENTUS

PDB ID 1iav

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