Reference : The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.
Scientific journals : Article
Life sciences : Microbiology
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/80432
The crystal structure of the beta-lactamase of Streptomyces albus G at 0.3 nm resolution.
English
Dideberg, Otto [Université de Liège - ULg > Institut de Physique > Laboratoire de Cristallographie > >]
Charlier, Paulette mailto [Université de Liège - ULg > Institut de Physique > Laboratoire de Cristallographie > >]
Wery, Jean-Paul [Université de Liège - ULg > Institut de Physique > Laboratoire de Cristallographie > >]
Dehottay, Philippe [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Dusart, Jean [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Erpicum, Thomas [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Institut de Chimie > Service de Microbiologie > > >]
1987
Biochemical Journal
Portland Press
245
3
911-913
Yes (verified by ORBi)
International
0264-6021
1470-8728
London
United Kingdom
[en] Models, Molecular ; Penicillinase ; Protein Conformation ; Streptomyces/enzymology ; X-Ray Diffraction
[en] 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.
Researchers ; Professionals
http://hdl.handle.net/2268/80432

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