1ios

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{{Seed}}
 
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[[Image:1ios.png|left|200px]]
 
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==STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION==
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The line below this paragraph, containing "STRUCTURE_1ios", creates the "Structure Box" on the page.
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<StructureSection load='1ios' size='340' side='right'caption='[[1ios]], [[Resolution|resolution]] 1.76&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'>[[1ios]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOS 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]] 1.76&#8491;</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=1ios FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ios OCA], [https://pdbe.org/1ios PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ios RCSB], [https://www.ebi.ac.uk/pdbsum/1ios PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ios ProSAT]</span></td></tr>
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{{STRUCTURE_1ios| PDB=1ios | SCENE= }}
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/LYSC_CHICK 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.<ref>PMID:22044478</ref>
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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/io/1ios_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1ios ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Stabilization 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.
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===STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION===
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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<ref>PMID:11266617</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1ios" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_11266617}}, adds the Publication Abstract to the page
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 11266617 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_11266617}}
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__TOC__
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</StructureSection>
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==About this Structure==
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1IOS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IOS OCA].
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==Reference==
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<ref group="xtra">PMID:11266617</ref><references group="xtra"/>
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[[Category: Gallus gallus]]
[[Category: Gallus gallus]]
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[[Category: Lysozyme]]
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[[Category: Large Structures]]
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[[Category: Imoto, T.]]
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[[Category: Imoto T]]
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[[Category: Ohmura, T.]]
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[[Category: Ohmura T]]
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[[Category: Ootsuka, K.]]
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[[Category: Ootsuka K]]
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[[Category: Saito, M.]]
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[[Category: Saito M]]
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[[Category: Ueda, T.]]
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[[Category: Ueda T]]
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[[Category: Bacteriolytic enzyme]]
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[[Category: Glycosidase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 12:15:27 2009''
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Current revision

STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION

PDB ID 1ios

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