1ysd
From Proteopedia
(Difference between revisions)
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<StructureSection load='1ysd' size='340' side='right'caption='[[1ysd]], [[Resolution|resolution]] 1.90Å' scene=''> | <StructureSection load='1ysd' size='340' side='right'caption='[[1ysd]], [[Resolution|resolution]] 1.90Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[1ysd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/ | + | <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=' | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.9Å</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=' | + | |
| - | + | ||
<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> | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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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=1ysd ConSurf]. | </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> | <div style="clear:both"></div> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | 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. | ||
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| - | Computational thermostabilization of an enzyme.,Korkegian A, Black ME, Baker D, Stoddard BL Science. 2005 May 6;308(5723):857-60. PMID:15879217<ref>PMID:15879217</ref> | ||
| - | |||
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 1ysd" style="background-color:#fffaf0;"></div> | ||
==See Also== | ==See Also== | ||
*[[Deaminase 3D structures|Deaminase 3D structures]] | *[[Deaminase 3D structures|Deaminase 3D structures]] | ||
| - | == References == | ||
| - | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
| - | [[Category: Atcc 18824]] | ||
| - | [[Category: Cytosine deaminase]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Saccharomyces cerevisiae]] |
| - | [[Category: | + | [[Category: Baker D]] |
| - | [[Category: | + | [[Category: Black ME]] |
| - | [[Category: | + | [[Category: Korkegian A]] |
| - | [[Category: | + | [[Category: Stoddard BL]] |
Current revision
Yeast Cytosine Deaminase Double Mutant
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