1yx9
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Effect of Dimethyl Sulphoxide on the crystal structure of Porcine Pepsin
OverviewOverview
The structure of porcine pepsin crystallized in the presence of dimethyl, sulphoxide has been analysed by X-ray crystallography to obtain insights, into the structural events that occur at the onset of chemical, denaturation of proteins. The results show that one dimethyl sulphoxide, molecule occupies a site on the surface of pepsin interacting with two of, its residues. An increase in the average temperature factor of pepsin in, the presence of dimethyl sulphoxide has been observed indicating protein, destabilization induced by the denaturant. Significant increase in the, temperature factor and weakening of the electron density have been, observed for the catalytic water molecule located between the active, aspartates. The conformation of pepsin remains unchanged in the crystal, structure. However, the enzyme assay and circular dichroism studies, indicate that dimethyl sulphoxide causes a slight change in the secondary, structure and complete loss of activity of pepsin in solution.
About this StructureAbout this Structure
1YX9 is a Single protein structure of sequence from Sus scrofa with DMS as ligand. Active as Pepsin A, with EC number 3.4.23.1 Full crystallographic information is available from OCA.
ReferenceReference
Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin., Kesavulu MM, Ramasubramanian S, Suguna K, Biochem Biophys Res Commun. 2005 Jun 17;331(4):1510-4. PMID:15883044
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