1YSB

Yeast Cytosine Deaminase Triple Mutant

Summary for 1YSB

Entry DOI	10.2210/pdb1ysb/pdb
Related	1YSD
Descriptor	Cytosine deaminase, ZINC ION, CALCIUM ION, ... (4 entities in total)
Functional Keywords	hydrolase
Biological source	Saccharomyces cerevisiae (baker's yeast)
Total number of polymer chains	2
Total formula weight	35936.38
Authors	Korkegian, A.,Black, M.E.,Baker, D.,Stoddard, B.L. (deposition date: 2005-02-08, release date: 2005-05-17, Last modification date: 2024-02-14)
Primary citation	Korkegian, A.,Black, M.E.,Baker, D.,Stoddard, B.L. Computational thermostabilization of an enzyme. Science, 308:857-860, 2005 Cited by PubMed Abstract: 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. PubMed: 15879217 DOI: 10.1126/science.1107387 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (1.7 Å)

Structure validation