- Abstract:
-
Colicin endonucleases (DNases) are bound and inactivated by immunity (Im) proteins. Im proteins are broadly cross-reactive yet specific inhibitors binding cognate and non-cognate DNases with K(d) values that vary between 10(-4) and 10(-14) M, characteristics that are explained by a 'dual-recognition' mechanism. In this work, we addressed for the first time the energetics of Im protein recognition by colicin DNases through a combination of E9 DNase alanine scanning and double-mutant cycles (DM...
Expand abstract - Publication status:
- Published
- Publisher copy:
- 10.1016/j.jmb.2008.03.055
-
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- Journal:
- Journal of molecular biology
- Volume:
- 379
- Issue:
- 4
- Pages:
- 745-759
- Publication date:
- 2008-06-05
- DOI:
- EISSN:
-
1089-8638
- ISSN:
-
0022-2836
- URN:
-
uuid:6a9cf90d-021c-4e76-90e2-fae688af1cff
- Source identifiers:
-
310203
- Local pid:
- pubs:310203
- Language:
- English
- Keywords:
- Copyright date:
- 2008
Journal article
Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.
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