1ADN

SOLUTION STRUCTURE OF THE DNA METHYLPHOSPHOTRIESTER REPAIR DOMAIN OF ESCHERICHIA COLI ADA

Summary for 1ADN

• Entry DOI: 10.2210/pdb1adn/pdb
• NMR Information: BMRB: 6053,6054
• Descriptor: N-ADA 10, ZINC ION (2 entities in total)
• Functional Keywords: transcription regulation
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 10535.39

Authors

Myers, L.C.,Verdine, G.L.,Wagner, G. (deposition date: 1993-09-30, release date: 1994-01-31, Last modification date: 2024-05-22)

Primary citation

Myers, L.C.,Verdine, G.L.,Wagner, G.
Solution structure of the DNA methyl phosphotriester repair domain of Escherichia coli Ada.
Biochemistry, 32:14089-14094, 1993

PubMed 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.

PubMed: 8260490
DOI: 10.1021/bi00214a003

Experimental method

SOLUTION NMR