Distinct conformational stability and functional activity of four highly homologous endonuclease colicins.

Journal article

The family of conserved colicin DNases E2, E7, E8, and E9 are microbial toxins that kill bacteria through random degradation of the chromosomal DNA. In the present work, we compare side by side the conformational stabilities of these four highly homologous colicin DNases. Our results indicate that the apo-forms of these colicins are at room temperature and neutral pH in a dynamic conformational equilibrium between at least two quite distinct conformers. We show that the thermal stabilities of...

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Authors: van den Bremer, E; Keeble, A; Jiskoot, W; Spelbrink, R; Maier, C

• Journal: Protein science : a publication of the Protein Society
• Volume: 13
• Issue: 5
• Pages: 1391-1401
• Publication date: 2004-05-01
• DOI: 10.1110/ps.03508204
• EISSN: 1469-896X
• ISSN: 0961-8368
• Language: English
• Keywords: Colicins; Amino Acid Sequence; Structural Homology, Protein; Endodeoxyribonucleases; Tryptophan; Enzyme Stability; Sequence Alignment; Calorimetry; Binding Sites; Spectrometry, Mass, Electrospray Ionization; Fluorescence; Molecular Sequence Data