1ir8

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Revision as of 15:28, 20 November 2007

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spinqualitylabelsall models 1ir8, resolution 1.63Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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. Active as Lysozyme, with EC number 3.2.1.17 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

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