1ysd: Difference between revisions

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-[[Image:1ysd.gif|left|200px]]<br /><applet load="1ysd" size="350" color="white" frame="true" align="right" spinBox="true"
-caption="1ysd, resolution 1.90&Aring;" />
-'''Yeast Cytosine Deaminase Double Mutant'''<br />
-==Overview==
+==Yeast Cytosine Deaminase Double Mutant==
-Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.
+<StructureSection load='1ysd' size='340' side='right'caption='[[1ysd]], [[Resolution|resolution]] 1.90&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1ysd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1YSD 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]] 1.9&#8491;</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></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=1ysd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ysd OCA], [https://pdbe.org/1ysd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ysd RCSB], [https://www.ebi.ac.uk/pdbsum/1ysd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ysd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/FCY1_YEAST FCY1_YEAST] Converts cytosine to uracil or 5-methylcytosine to thymine by deaminating carbon number 4.
+== 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/ys/1ysd_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=1ysd ConSurf].
+<div style="clear:both"></div>
-==About this Structure==
+==See Also==
-YSD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=ZN:'>ZN</scene> and <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cytosine_deaminase Cytosine deaminase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.5.4.1 3.5.4.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YSD OCA].
+*[[Deaminase 3D structures|Deaminase 3D structures]]
+__TOC__
-==Reference==
+</StructureSection>
-Computational thermostabilization of an enzyme., Korkegian A, Black ME, Baker D, Stoddard BL, Science. 2005 May 6;308(5723):857-60. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15879217 15879217]
+[[Category: Large Structures]]
-[[Category: Cytosine deaminase]]
 [[Category: Saccharomyces cerevisiae]]
-[[Category: Single protein]]
+[[Category: Baker D]]
-[[Category: Baker, D.]]
+[[Category: Black ME]]
-[[Category: Black, M E.]]
+[[Category: Korkegian A]]
-[[Category: Korkegian, A.]]
+[[Category: Stoddard BL]]
-[[Category: Stoddard, B L.]]
-[[Category: CA]]
-[[Category: ZN]]
-[[Category: cytosine deaminase]]
-[[Category: hydrolase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:08:40 2008''