1ir8

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(New page: 200px<br /><applet load="1ir8" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ir8, resolution 1.63&Aring;" /> '''IM mutant of lysozym...)
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[[Image:1ir8.jpg|left|200px]]<br /><applet load="1ir8" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ir8, resolution 1.63&Aring;" />
 
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'''IM mutant of lysozyme'''<br />
 
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==Overview==
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==IM mutant of lysozyme==
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X-ray structure determination of proteins by using the multiple-wavelength, anomalous dispersion method targeting selenomethionine is now widely, employed. Isoleucine was examined for the second choice of the, substitution of methionine next to leucine. We performed a systematic, mutational study of the substitutions of methionine for isoleucine. All, mutated lysozymes were less stable than the wild-type by about 1 kcal/mol, and it is suggested that this instability was caused by the change in, residual hydrophobicity from isoleucine to methionine. The X-ray, structures of all mutant lysozymes were very similar to that of the, wild-type. In addition, both the accessible surface areas and the, conformation of the side chain of methionine in all mutant lysozymes were, similar to those of the side chain at the respective isoleucine in the, wild-type. Therefore, it is suggested that the mutation from isoleucine to, methionine in a protein can be considered as a "safe" substitution.
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<StructureSection load='1ir8' size='340' side='right'caption='[[1ir8]], [[Resolution|resolution]] 1.63&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ir8]] 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=1IR8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IR8 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]] 1.63&#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=1ir8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ir8 OCA], [https://pdbe.org/1ir8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ir8 RCSB], [https://www.ebi.ac.uk/pdbsum/1ir8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ir8 ProSAT]</span></td></tr>
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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/ir/1ir8_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=1ir8 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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X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution.
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==About this Structure==
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Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme.,Ohmura T, Ueda T, Hashimoto Y, Imoto T Protein Eng. 2001 Jun;14(6):421-5. PMID:11477222<ref>PMID:11477222</ref>
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1IR8 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [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] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1IR8 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme., Ohmura T, Ueda T, Hashimoto Y, Imoto T, Protein Eng. 2001 Jun;14(6):421-5. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11477222 11477222]
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</div>
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[[Category: Gallus gallus]]
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<div class="pdbe-citations 1ir8" style="background-color:#fffaf0;"></div>
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[[Category: Lysozyme]]
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[[Category: Single protein]]
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[[Category: Hashimoto, Y.]]
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[[Category: Imoto, T.]]
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[[Category: Ohmura, T.]]
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[[Category: Ueda, T.]]
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[[Category: egg white]]
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[[Category: hydrolase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:36:05 2007''
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==See Also==
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*[[Lysozyme 3D structures|Lysozyme 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Gallus gallus]]
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[[Category: Large Structures]]
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[[Category: Hashimoto Y]]
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[[Category: Imoto T]]
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[[Category: Ohmura T]]
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[[Category: Ueda T]]

Current revision

IM mutant of lysozyme

PDB ID 1ir8

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