Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada.

Abstract:

:The Escherichia coli Ada protein repairs methyl phosphotriesters in DNA by direct, irreversible methyl transfer to one of its own cysteine residues. The methyl-transfer process appears to be autocatalyzed by coordination of the acceptor residue, Cys-69, to a tightly bound zinc ion. Upon methyl transfer, Ada acquires the ability to bind DNA sequence-specifically and thereby to induce genes that confer resistance to methylating agents. The solution structure of an N-terminal 10-kDa fragment of Ada, which retains zinc binding and DNA methyl phosphotriester repair activities, was determined using multidimensional heteronuclear nuclear magnetic resonance techniques. The structure reveals a zinc-binding motif unlike any observed thus far in transcription factors or zinc-containing enzymes and provides insight into the mechanism of metalloactivated DNA repair.

journal_name

Biochemistry

journal_title

Biochemistry

authors

Myers LC,Verdine GL,Wagner G

doi

10.1021/bi00214a003

subject

Has Abstract

pub_date

1993-12-28 00:00:00

pages

14089-94

issue

51

eissn

0006-2960

issn

1520-4995

journal_volume

32

pub_type

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