Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold

Citation
B. Hocker et al., Stability, catalytic versatility and evolution of the (beta alpha)(8)-barrel fold, CURR OPIN B, 12(4), 2001, pp. 376-381
Citations number
39
Categorie Soggetti
Microbiology
Journal title
CURRENT OPINION IN BIOTECHNOLOGY
ISSN journal
09581669 → ACNP
Volume
12
Issue
4
Year of publication
2001
Pages
376 - 381
Database
ISI
SICI code
0958-1669(200108)12:4<376:SCVAEO>2.0.ZU;2-R
Abstract
The (beta alpha)(8)-barrel is a versatile single-domain protein fold that i s 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 thermost ability and in studies to interconvert catalytic activities or substrate sp ecificities by rational design or directed evolution. Recently, the (beta a lpha)(4)-half-barrel was identified as a possible structural subdomain.