1ysb

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|PDB= 1ysb |SIZE=350|CAPTION= <scene name='initialview01'>1ysb</scene>, resolution 1.70&Aring;
|PDB= 1ysb |SIZE=350|CAPTION= <scene name='initialview01'>1ysb</scene>, resolution 1.70&Aring;
|SITE=
|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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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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|ACTIVITY= [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]
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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>
|GENE= FCY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
|GENE= FCY1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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|RELATEDENTRY=[[1ysd|1YSD]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ysb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ysb OCA], [http://www.ebi.ac.uk/pdbsum/1ysb PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ysb RCSB]</span>
}}
}}
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[[Category: Korkegian, A.]]
[[Category: Korkegian, A.]]
[[Category: Stoddard, B L.]]
[[Category: Stoddard, B L.]]
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[[Category: CA]]
 
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[[Category: ZN]]
 
[[Category: hydrolase]]
[[Category: hydrolase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 01:20:14 2008''

Revision as of 22:20, 30 March 2008


PDB ID 1ysb

Drag the structure with the mouse to rotate
, resolution 1.70Å
Ligands: ,
Gene: FCY1 (Saccharomyces cerevisiae)
Activity: Cytosine deaminase, with EC number 3.5.4.1
Related: 1YSD


Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



Yeast Cytosine Deaminase Triple 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

1YSB 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

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