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Journal article

Experimental and computational analyses of the energetic basis for dual recognition of immunity proteins by colicin endonucleases.

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...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2008.03.055

Authors


Keeble, AH More by this author
Joachimiak, LA More by this author
Kirkpatrick, N More by this author
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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

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