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Multistep binding of transition metals to the H-N-H endonuclease toxin colicin E9.

Abstract:

We report the first stopped-flow fluorescence analysis of transition metal binding (Co(2+), Ni(2+), Cu(2+), and Zn(2+)) to the H-N-H endonuclease motif within colicin E9 (the E9 DNase). The H-N-H consensus forms the active site core of a number of endonuclease groups but is also structurally homologous to the so-called treble-clef motif, a ubiquitous zinc-binding motif found in a wide variety of metalloproteins. We find that all the transition metal ions tested bind via multistep mechanisms. ...

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Publisher copy:
10.1021/bi020174o

Authors


Keeble, AH More by this author
Hemmings, AM More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
Journal:
Biochemistry
Volume:
41
Issue:
32
Pages:
10234-10244
Publication date:
2002-08-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:58f8a115-f9f5-481c-a80e-7a4b93fcf3fd
Source identifiers:
310236
Local pid:
pubs:310236

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