1ir7: Difference between revisions

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-[[Image:1ir7.jpg|left|200px]]
- {{Structure
+==IM mutant of lysozyme==
-|PDB= 1ir7 |SIZE=350|CAPTION= <scene name='initialview01'>1ir7</scene>, resolution 1.9&Aring;
+<StructureSection load='1ir7' size='340' side='right'caption='[[1ir7]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND=
+<table><tr><td colspan='2'>[[1ir7]] 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=1IR7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IR7 FirstGlance]. <br>
-|ACTIVITY= <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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9&#8491;</td></tr>
-|GENE=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ir7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ir7 OCA], [https://pdbe.org/1ir7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ir7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ir7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ir7 ProSAT]</span></td></tr>
-|DOMAIN=
+</table>
-|RELATEDENTRY=[[1ir8|1IR8]], [[1ir9|1IR9]]
+== Function ==
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ir7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ir7 OCA], [http://www.ebi.ac.uk/pdbsum/1ir7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ir7 RCSB]</span>
+[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>
-}}
+== Evolutionary Conservation ==
+[[Image:Consurf_key_small.gif|200px|right]]
+Check<jmol>
+  <jmolCheckbox>
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ir/1ir7_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
+  </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/main_output.php?pdb_ID=1ir7 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-'''IM mutant of lysozyme'''
+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>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1ir7" style="background-color:#fffaf0;"></div>
-==Overview==
+==See Also==
-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.
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
-==About this Structure==
+<references/>
-IR7 is a [[Single protein]] 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=1IR7 OCA].
+__TOC__
+</StructureSection>
-==Reference==
-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://www.ncbi.nlm.nih.gov/pubmed/11477222 11477222]
 [[Category: Gallus gallus]]
-[[Category: Lysozyme]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Hashimoto Y]]
-[[Category: Hashimoto, Y.]]
+[[Category: Imoto T]]
-[[Category: Imoto, T.]]
+[[Category: Ohmura T]]
-[[Category: Ohmura, T.]]
+[[Category: Ueda T]]
-[[Category: Ueda, T.]]
-[[Category: egg white]]
-[[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:23:29 2008''