Open AccessStudy of the Zn‐containing dd ‐carboxypeptidase of Streptomyces albus G by small‐angle X‐ray scattering in solution
Author(s) -
LABISCHINSKI Harald,
GIESBRECHT Peter,
FISCHER Erwin,
BARNICKEL Gerhard,
BRADACZEK Hans,
FRÈRE JeanMarie,
HOUSSIER Claude,
CHARLIER Paulette,
DIDEBERG Otto,
GHUYSEN JeanMarie
Publication year - 1984
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1984.tb07884.x
Subject(s) - radius of gyration , streptomyces albus , scattering , small angle x ray scattering , chemistry , crystallography , gyration , carboxypeptidase , hydrodynamic radius , radius , small angle scattering , stereochemistry , enzyme , streptomyces , aqueous solution , physics , biochemistry , organic chemistry , geometry , polymer , optics , biology , micelle , bacteria , mathematics , computer security , computer science , genetics
Study of the Zn 2+ ‐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 M r = 17000 ± 2000; volume V ∼ 35 ± 2 nm 3 ; 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 β‐lactam inhibitors, cephalothin and cephalosporin C, drastically altered the scattering behaviour of the protein.