1ioq: Difference between revisions

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:1ioq.gif|left|200px]]<br /><applet load="1ioq" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1ioq, resolution 1.79&Aring;" />
-'''STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION'''<br />
-==Overview==
+==STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY-FILLING MUTATION==
-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.
+<StructureSection load='1ioq' size='340' side='right'caption='[[1ioq]], [[Resolution|resolution]] 1.79&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ioq]] 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=1IOQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IOQ FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.79&#8491;</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=1ioq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ioq OCA], [https://pdbe.org/1ioq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ioq RCSB], [https://www.ebi.ac.uk/pdbsum/1ioq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ioq ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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/io/1ioq_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.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=1ioq ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+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.
-==About this Structure==
+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>
-IOQ 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=1IOQ OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11266617 11266617]
+</div>
+<div class="pdbe-citations 1ioq" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Lysozyme 3D structures|Lysozyme 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Gallus gallus]]
-[[Category: Lysozyme]]
+[[Category: Large Structures]]
-[[Category: Single protein]]
+[[Category: Imoto T]]
-[[Category: Imoto, T.]]
+[[Category: Ohmura T]]
-[[Category: Ohmura, T.]]
+[[Category: Ootsuka K]]
-[[Category: Ootsuka, K.]]
+[[Category: Saito M]]
-[[Category: Saito, M.]]
+[[Category: Ueda T]]
-[[Category: Ueda, T.]]
-[[Category: bacteriolytic enzyme]]
-[[Category: glycosidase]]
-[[Category: hydrolase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:33:06 2007''