1jea
From Proteopedia
(Difference between revisions)
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<StructureSection load='1jea' size='340' side='right'caption='[[1jea]], [[Resolution|resolution]] 2.00Å' scene=''> | <StructureSection load='1jea' size='340' side='right'caption='[[1jea]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1jea]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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> |
| - | </td></tr><tr id=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2Å</td></tr> |
| - | <tr id=' | + | <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> |
<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> | <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> | ||
</table> | </table> | ||
== Function == | == Function == | ||
| - | + | [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. | |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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]. | </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]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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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| - | 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:10493860<ref>PMID:10493860</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1jea" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Subtilisin 3D structures|Subtilisin 3D structures]] | *[[Subtilisin 3D structures|Subtilisin 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 10840]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Lederbergia lenta]] |
| - | [[Category: Bott | + | [[Category: Bott R]] |
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Current revision
ALTERED TOPOLOGY AND FLEXIBILITY IN ENGINEERED SUBTILISIN
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