1YX9
Effect of Dimethyl Sulphoxide on the crystal structure of Porcine Pepsin
Summary for 1YX9
| Entry DOI | 10.2210/pdb1yx9/pdb |
| Related | 4pep 5pep |
| Descriptor | pepsinogen A, DIMETHYL SULFOXIDE (3 entities in total) |
| Functional Keywords | pepsin, dimethyl sulphoxide, protein denaturation, hydrolase |
| Biological source | Sus scrofa (pig) |
| Total number of polymer chains | 1 |
| Total formula weight | 34591.64 |
| Authors | Kesavulu, M.M.,Ramasubramanian, S.,Suguna, K. (deposition date: 2005-02-20, release date: 2005-05-24, Last modification date: 2024-10-30) |
| Primary citation | Kesavulu, M.M.,Ramasubramanian, S.,Suguna, K. Effect of dimethyl sulphoxide on the crystal structure of porcine pepsin. Biochem.Biophys.Res.Commun., 331:1510-1514, 2005 Cited by PubMed Abstract: 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. PubMed: 15883044DOI: 10.1016/j.bbrc.2005.03.247 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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