Reference : Study of the Zn-containing DD-carboxypeptidase of Streptomyces albus G by small-angle X-...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/80433
Study of the Zn-containing DD-carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution.
English
Labischinski, Harald [Robert-Koch-Institut des Bundesgesundheitsamtes > > > > > >]
Giesbrecht, Peter [Robert-Koch-Institut des Bundesgesundheitsamtes > > > > > >]
Fischer, E. [Institut Für Kristallographie der Freien Universität Berlin > > > >]
Barnickel, G. [Institut Für Kristallographie der Freien Universität Berlin > > > > > >]
Bradaczek, H. [Institut Für Kristallographie der Freien Universität Berlin > > > > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie Organique et de Biochimie > Laboratoire de Microbiologie > >]
Houssier, Claude mailto [Université de Liège - ULg > Institut de Chimie > Laboratoire de Chimie Physique > >]
Charlier, Paulette mailto [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie Organique et de Biochimie > Laboratoire de Microbiologie > >]
Dideberg, Otto [Université de Liège - ULg > Institut de Physique > Laboratoire de Cristallographie > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > Faculté de Médecine, Institut de Chimie Organique et de Biochimie > Laboratoire de Microbiologie > >]
1984
European Journal of Biochemistry
Blackwell Science
138
1
83-87
Yes (verified by ORBi)
International
0014-2956
1432-1033
Oxford
United Kingdom
[en] Carboxypeptidases/analysis ; Cephalosporins ; Cephalothin ; Chemical Phenomena ; Chemistry ; Fluorescence Polarization ; Molecular Weight ; Scattering, Radiation ; Solutions ; Streptomyces/enzymology ; X-Rays
[en] Study of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution yielded the following molecular parameters: radius of gyration R = 1.82 +/- 0.05 nm; largest diameter D = 5.9 +/- 0.2 nm; relative molecular mass Mr = 17000 +/- 2000; volume V approximately equal to 35 +/- 2 nm3; degree of hydration: 0.25 +/- 0.02 g water/g protein. By reference to theoretical scattering curves of rigid triaxial homogeneous bodies, a model which fits all experimental data is an elliptical cylinder. Such a model is compatible with that observed in the crystal structure. At those high concentrations necessary to form inactive enzyme-ligand associations the non-competitive beta-lactam inhibitors, cephalothin and cephalosporin C, drastically altered the scattering behaviour of the protein.
Fonds de la Recherche Scientifique Médicale - FRSM
Researchers ; Professionals
http://hdl.handle.net/2268/80433

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