Functional Tolerance of Streptomyces Subtilisin Inhibitor toward Conformational and Stability Changes Caused by Single-Point Mutations in the Hydrophobic Core.

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概要

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• Single amino acid mutations of Met103 in the hydrophobic core of a serine protease inhibitor, Streptomyces subtilisin inhibitor, caused little change in the inhibitory activity, as measured by the inhibitor constant, although some altered the thermodynamic stability of the protein considerably. 1H NMR investigations showed that the conformational stress caused by the replacement of Met103 with Gly, Ala, Val, and Ile, namely, the effects of the cavities generated by replacements with smaller side-chains and of the steric distortions generated by β-branched side-chains, caused considerable changes in the structural arrangement of the side-chains within the core. However, these structural changes were absorbed within the hydrophobic core, without distorting the structure of the reactive site essential for the protein function. These results provide an excellent example of the conformational flexibility of a protein core and the degree of its tolerance of an amino acid replacement. The results also reveal the crucially designed structural relationship between the core of the inhibitor and the enzyme-binding segment with the reactive site in a serine protease inhibitor.

• 社団法人 日本生化学会の論文

著者

• MOMMA KEIKO

  Department of Basic and Applied Molecular Biotechnology, Division of Food and Biological Science, Gr

• Tamura Atsuo

  Graduate School Of Science And Technology Kobe Univ.

• Kanaori Kenji

  Department Of Applied Biology Kyoto Institute Of Technology

• Kojima Shuichi

  Institute For Biomolecular Science Faculty Of Science Gakushuin University

• Akasaka Kazuyuki

  Department Of Biotechnological Science School Of Biology-oriented Science And Technology Kinki Unive

• Miura Kin-ichiro

  Institute For Biomolecular Science Faculty Of Science Gakushuin University

• Oda Masayuki

  Research Institute For Biological Sciences Tokyo University Of Science

• KOJIMA Shuichi

  Institute of Biomolecular Science, Gakushuin University

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