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1IR8

IM mutant of lysozyme

Summary for 1IR8
Entry DOI10.2210/pdb1ir8/pdb
Related1IR7 1IR9
Descriptorlysozyme (2 entities in total)
Functional Keywordshydrolase, egg white
Biological sourceGallus gallus (chicken)
Cellular locationSecreted: P00698
Total number of polymer chains1
Total formula weight14349.20
Authors
Ohmura, T.,Ueda, T.,Hashimoto, Y.,Imoto, T. (deposition date: 2001-09-19, release date: 2001-10-03, Last modification date: 2023-12-27)
Primary citationOhmura, T.,Ueda, T.,Hashimoto, Y.,Imoto, T.
Tolerance of point substitution of methionine for isoleucine in hen egg white lysozyme.
Protein Eng., 14:421-425, 2001
Cited by
PubMed Abstract: 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.
PubMed: 11477222
DOI: 10.1093/protein/14.6.421
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.63 Å)
Structure validation

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