| Literature DB >> 3499147 |
O Dideberg1, P Charlier, J P Wéry, P Dehottay, J Dusart, T Erpicum, J M Frère, J M Ghuysen.
Abstract
The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains.Entities:
Mesh:
Substances:
Year: 1987 PMID: 3499147 PMCID: PMC1148217 DOI: 10.1042/bj2450911
Source DB: PubMed Journal: Biochem J ISSN: 0264-6021 Impact factor: 3.857