PMID: 638183Mar 28, 1978

Conformation of a stable intermediate on the folding pathway of Staphylococcus aureus penicillinase

Biochimica Et Biophysica Acta
E A Carrey, R H Pain

Abstract

The partly unfolded intermediate (state H) of penicillinase from Staphylococcus aureus PC1 is stable in 0.8 M guanidinium chloride at pH 7.0. It has been characterized by measurements of intrinsic viscosity, sedimentation and diffusion coefficients, leading to an equivalent hydrodynamic volume of five times that of the native penicillinase molecule. Values of alpha-helix content calculated from circular dichroism were 27% for penicillinase and 16% for state H. A multi-domain model is proposed for penicillinase in which the domains can separate without appreciable change in secondary structure. This model is important in understanding the means by which the enzyme activity can be controlled, and corresponds to a kinetic pathway of folding.

References

Jun 18, 1974·Biochemistry·K P Wong, L M Hamlin
Dec 1, 1971·Annals of Internal Medicine·M Robson, J B Rosenfeld
Mar 1, 1964·Biochemistry·D A YPHANTIS

Citations

Nov 1, 1993·Protein Science : a Publication of the Protein Society·C J MannC R Matthews
Dec 5, 1991·Journal of Molecular Biology·D J Thomas
Feb 15, 1980·Journal of Molecular Biology·T E Creighton
Mar 15, 1980·Journal of Molecular Biology·T E Creighton, R H Pain
Apr 1, 1984·Analytical Biochemistry·D P Goldenberg, T E Creighton
Nov 1, 1981·European Journal of Biochemistry·W Slobbe, G Voordouw
Apr 6, 2013·Acta Biochimica Et Biophysica Sinica·Pei HuangDonghai Lin
May 16, 1980·Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences·R BucourtJ Perronnet

Related Concepts

Circular Dichroism, Vibrational
Diffusion
Guanidines
Optical Rotation
Exopenicillinase
Protein Conformation
Staphylococcus aureus
Ultracentrifugation
Carmol
Viscosity

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