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==STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION== | ==STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION== | ||
<StructureSection load='1ior' size='340' side='right' caption='[[1ior]], [[Resolution|resolution]] 1.76Å' scene=''> | <StructureSection load='1ior' size='340' side='right' caption='[[1ior]], [[Resolution|resolution]] 1.76Å' scene=''> | ||
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</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ioq|1ioq]], [[1ios|1ios]], [[1iot|1iot]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ioq|1ioq]], [[1ios|1ios]], [[1iot|1iot]]</td></tr> | ||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | <tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] </span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ior OCA], [http://pdbe.org/1ior PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ior RCSB], [http://www.ebi.ac.uk/pdbsum/1ior PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ior FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ior OCA], [http://pdbe.org/1ior PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ior RCSB], [http://www.ebi.ac.uk/pdbsum/1ior PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ior ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </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/ | </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=1ior ConSurf]. | ||
<div style="clear:both"></div> | <div style="clear:both"></div> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
Revision as of 12:43, 4 October 2017
STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATIONSTABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION
Structural highlights
Function[LYSC_CHICK] Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. Has bacteriolytic activity against M.luteus.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedStabilization of a protein using cavity-filling strategy has hardly been successful because of unfavorable van der Waals contacts. We succeeded in stabilizing lysozymes by cavity-filling mutations. The mutations were checked by a simple energy minimization in advance. It was shown clearly that the sum of free energy change caused by the hydrophobicity and the cavity size was correlated very well with protein stability. We also considered the aromatic-aromatic interaction. It is reconfirmed that the cavity-filling mutation in a hydrophobic core is a very useful method to stabilize a protein when the mutation candidate is selected carefully. Stabilization of hen egg white lysozyme by a cavity-filling mutation.,Ohmura T, Ueda T, Ootsuka K, Saito M, Imoto T Protein Sci. 2001 Feb;10(2):313-20. PMID:11266617[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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