1ysd

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[[Image:1ysd.gif|left|200px]]
[[Image:1ysd.gif|left|200px]]
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{{Structure
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<!--
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|PDB= 1ysd |SIZE=350|CAPTION= <scene name='initialview01'>1ysd</scene>, resolution 1.90&Aring;
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The line below this paragraph, containing "STRUCTURE_1ysd", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY= <span class='plainlinks'>[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] </span>
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or leave the SCENE parameter empty for the default display.
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|GENE= FCY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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-->
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|DOMAIN=
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{{STRUCTURE_1ysd| PDB=1ysd | SCENE= }}
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|RELATEDENTRY=[[1ysb|1YSB]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ysd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ysd OCA], [http://www.ebi.ac.uk/pdbsum/1ysd PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ysd RCSB]</span>
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}}
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'''Yeast Cytosine Deaminase Double Mutant'''
'''Yeast Cytosine Deaminase Double Mutant'''
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[[Category: Korkegian, A.]]
[[Category: Korkegian, A.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
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[[Category: cytosine deaminase]]
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[[Category: Cytosine deaminase]]
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[[Category: hydrolase]]
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[[Category: Hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:43:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:20:39 2008''
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Revision as of 13:43, 3 May 2008

Image:1ysd.gif

Template:STRUCTURE 1ysd

Yeast Cytosine Deaminase Double Mutant


Overview

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.

About this Structure

1YSD is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Computational thermostabilization of an enzyme., Korkegian A, Black ME, Baker D, Stoddard BL, Science. 2005 May 6;308(5723):857-60. PMID:15879217 Page seeded by OCA on Sat May 3 16:43:21 2008

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OCA

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