title: Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold.
abstract: 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.
authors.affiliation: Universität zu Köln, Institut für Biochemie, Otto-Fischer-Strasse 12-14, D-50674 Köln, Germany.
authors.forename: B
authors.initials: B
authors.lastname: Höcker
authors.forename: C
authors.initials: C
authors.lastname: Jürgens
authors.forename: M
authors.initials: M
authors.lastname: Wilmanns
authors.forename: R
authors.initials: R
authors.lastname: Sterner
mesh_terms: 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
chemical_list: D010751:Phosphopyruvate Hydratase