1wld: Difference between revisions

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-{{Seed}}
-[[Image:1wld.png|left|200px]]
-<!--
+==Congerin II T88I single mutant==
-The line below this paragraph, containing "STRUCTURE_1wld", creates the "Structure Box" on the page.
+<StructureSection load='1wld' size='340' side='right'caption='[[1wld]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<table><tr><td colspan='2'>[[1wld]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WLD FirstGlance]. <br>
-or leave the SCENE parameter empty for the default display.
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.6&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BGC:BETA-D-GLUCOSE'>BGC</scene>, <scene name='pdbligand=GAL:BETA-D-GALACTOSE'>GAL</scene>, <scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=PRD_900004:beta-lactose'>PRD_900004</scene></td></tr>
-{{STRUCTURE_1wld|  PDB=1wld  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1wld FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wld OCA], [https://pdbe.org/1wld PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wld RCSB], [https://www.ebi.ac.uk/pdbsum/1wld PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wld ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/LEG2_CONMY LEG2_CONMY] This protein binds beta-galactoside. Its physiological function is not yet known.
+== 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/wl/1wld_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=1wld ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The thermostability of the conger eel galectin, congerin II, was improved by in vitro evolutionary protein engineering. Two rounds of random PCR mutagenesis and selection experiments increased the congerin II thermostability to a level comparative to its naturally thermostable isoform, congerin I. The crystal structures of the most thermostable double mutant, Y16S/T88I, and the related single mutants, Y16S and T88I, were determined at 2.0 angstroms, 1.8 angstroms, and 1.6 angstroms resolution, respectively. The exclusion of two interior water molecules by the Thr88Ile mutation, and the relief of adjacent conformational stress by the Tyr16Ser mutation were the major contributions to the thermostability. These features in the congerin II mutants are similar to those observed in congerin I. The natural evolution of congerin genes, with the K(A)/K(S) ratio of 2.6, was accelerated under natural selection pressures. The thermostabilizing selection pressure artificially applied to congerin II mimicked the implied natural pressure on congerin I. The results showed that the artificial pressure made congerin II partially reproduce the natural evolution of congerin I.
-===Congerin II T88I single mutant===
+In vitro evolutionary thermostabilization of congerin II: a limited reproduction of natural protein evolution by artificial selection pressure.,Shionyu-Mitsuyama C, Ito Y, Konno A, Miwa Y, Ogawa T, Muramoto K, Shirai T J Mol Biol. 2005 Mar 25;347(2):385-97. Epub 2005 Jan 27. PMID:15740748<ref>PMID:15740748</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_15740748}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1wld" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 15740748 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_15740748}}
+__TOC__
+</StructureSection>
-==About this Structure==
-WLD is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Conger_myriaster Conger myriaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WLD OCA].
-==Reference==
-<ref group="xtra">PMID:15740748</ref><references group="xtra"/>
 [[Category: Conger myriaster]]
-[[Category: Ito, Y.]]
+[[Category: Large Structures]]
-[[Category: Konno, A.]]
+[[Category: Ito Y]]
-[[Category: Miwa, Y.]]
+[[Category: Konno A]]
-[[Category: Muramoto, K.]]
+[[Category: Miwa Y]]
-[[Category: Ogawa, T.]]
+[[Category: Muramoto K]]
-[[Category: Shionyu-Mitsuyama, C.]]
+[[Category: Ogawa T]]
-[[Category: Shirai, T.]]
+[[Category: Shionyu-Mitsuyama C]]
-[[Category: Beta-sandwich]]
+[[Category: Shirai T]]
-[[Category: Galectin]]
-[[Category: Mutant]]
-[[Category: Sugar binding protein]]
-[[Category: Thermostability]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Aug  5 09:08:16 2009''