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.
The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution
- Views Icon Views
- PDF LinkPDF
- Share Icon Share
- Cite Icon Cite
O Dideberg, P Charlier, J P Wéry, P Dehottay, J Dusart, T Erpicum, J M Frère, J M Ghuysen; The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution. Biochem J 1 August 1987; 245 (3): 911–913. doi: https://doi.org/10.1042/bj2450911
Download citation file: