Document Detail

In vitro evolutionary thermostabilization of congerin II: a limited reproduction of natural protein evolution by artificial selection pressure.
MedLine Citation:
PMID:  15740748     Owner:  NLM     Status:  MEDLINE    
The thermostability of the conger eel galectin, congerin II, was improved by in vitro evolutionary protein engineering. Two rounds of random PCR mutagenesis and selection experiments increased the congerin II thermostability to a level comparative to its naturally thermostable isoform, congerin I. The crystal structures of the most thermostable double mutant, Y16S/T88I, and the related single mutants, Y16S and T88I, were determined at 2.0 angstroms, 1.8 angstroms, and 1.6 angstroms resolution, respectively. The exclusion of two interior water molecules by the Thr88Ile mutation, and the relief of adjacent conformational stress by the Tyr16Ser mutation were the major contributions to the thermostability. These features in the congerin II mutants are similar to those observed in congerin I. The natural evolution of congerin genes, with the K(A)/K(S) ratio of 2.6, was accelerated under natural selection pressures. The thermostabilizing selection pressure artificially applied to congerin II mimicked the implied natural pressure on congerin I. The results showed that the artificial pressure made congerin II partially reproduce the natural evolution of congerin I.
Clara Shionyu-Mitsuyama; Yoshimaro Ito; Ayumu Konno; Yukiko Miwa; Tomohisa Ogawa; Koji Muramoto; Tsuyoshi Shirai
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2005-01-27
Journal Detail:
Title:  Journal of molecular biology     Volume:  347     ISSN:  0022-2836     ISO Abbreviation:  J. Mol. Biol.     Publication Date:  2005 Mar 
Date Detail:
Created Date:  2005-03-02     Completed Date:  2005-04-18     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  2985088R     Medline TA:  J Mol Biol     Country:  England    
Other Details:
Languages:  eng     Pagination:  385-97     Citation Subset:  IM    
Department of Computational Biology, Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
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MeSH Terms
Amino Acid Sequence
Base Sequence
Crystallography, X-Ray
Evolution, Molecular*
Galectins* / chemistry,  genetics,  metabolism
Models, Molecular
Molecular Sequence Data
Protein Isoforms* / chemistry,  genetics,  metabolism
Protein Structure, Tertiary*
Selection, Genetic*
Sequence Alignment
Reg. No./Substance:
0/Galectins; 0/Protein Isoforms; 0/congerin II protein, Conger eel

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