The crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution

Author:

Dideberg O1,Charlier P1,Wéry J P1,Dehottay P1,Dusart J1,Erpicum T1,Frère J M1,Ghuysen J M1

Affiliation:

1. Laboratoire de Cristalographie, Institut de Physique, University of Liège, Belgium.

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.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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