1ir8
From Proteopedia
IM mutant of lysozyme
Overview
X-ray structure determination of proteins by using the multiple-wavelength anomalous dispersion method targeting selenomethionine is now widely employed. Isoleucine was examined for the second choice of the substitution of methionine next to leucine. We performed a systematic mutational study of the substitutions of methionine for isoleucine. All mutated lysozymes were less stable than the wild-type by about 1 kcal/mol and it is suggested that this instability was caused by the change in residual hydrophobicity from isoleucine to methionine. The X-ray structures of all mutant lysozymes were very similar to that of the wild-type. In addition, both the accessible surface areas and the conformation of the side chain of methionine in all mutant lysozymes were similar to those of the side chain at the respective isoleucine in the wild-type. Therefore, it is suggested that the mutation from isoleucine to methionine in a protein can be considered as a "safe" substitution.
About this Structure
1IR8 is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme., Ohmura T, Ueda T, Hashimoto Y, Imoto T, Protein Eng. 2001 Jun;14(6):421-5. PMID:11477222 Page seeded by OCA on Fri May 2 20:18:56 2008
Categories: Gallus gallus | Lysozyme | Single protein | Hashimoto, Y. | Imoto, T. | Ohmura, T. | Ueda, T. | Egg white | Hydrolase
