1ir9: Difference between revisions
New page: left|200px<br /><applet load="1ir9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ir9, resolution 1.9Å" /> '''IM mutant of lysozyme... |
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[[Image:1ir9.jpg|left|200px]]<br /><applet load="1ir9" size=" | [[Image:1ir9.jpg|left|200px]]<br /><applet load="1ir9" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1ir9, resolution 1.9Å" /> | caption="1ir9, resolution 1.9Å" /> | ||
'''IM mutant of lysozyme'''<br /> | '''IM mutant of lysozyme'''<br /> | ||
==Overview== | ==Overview== | ||
X-ray structure determination of proteins by using the multiple-wavelength | 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== | ==About this Structure== | ||
1IR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http:// | 1IR9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Gallus_gallus Gallus gallus]. Active as [http://en.wikipedia.org/wiki/Lysozyme Lysozyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.17 3.2.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IR9 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: hydrolase]] | [[Category: hydrolase]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:14:48 2008'' | ||
Revision as of 14:14, 21 February 2008
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IM mutant of lysozyme
OverviewOverview
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 StructureAbout this Structure
1IR9 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.
ReferenceReference
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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