Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold.
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that is adopted by a large number of enzymes. The (beta alpha)(8)-barrel fold has been used as a model to elucidate the structural basis of protein thermostability and in studies to interconvert catalytic activities or substrate specificities by rational design or directed evolution. Recently, the (beta alpha)(4)-half-barrel was identified as a possible structural subdomain.
Höcker
B
B
Universität zu Köln, Institut für Biochemie, Otto-Fischer-Strasse 12-14, D-50674 Köln, Germany.
Jürgens
C
C
Wilmanns
M
M
Sterner
R
R
D002384:Catalysis; D019020:Directed Molecular Evolution / Q000379:methods*; D019143:Evolution, Molecular; D010751:Phosphopyruvate Hydratase / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D017433:Protein Structure, Secondary; D013379:Substrate Specificity; D013816:Thermodynamics
D010751:Phosphopyruvate Hydratase