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PDBsum entry 1adn

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Transcription regulation PDB id
1adn
Contents
Protein chain
92 a.a.
Metals
_ZN

References listed in PDB file
Key reference
Title Solution structure of the DNA methyl phosphotriester repair domain of escherichia coli ada.
Authors L.C.Myers, G.L.Verdine, G.Wagner.
Ref. Biochemistry, 1993, 32, 14089-14094. [DOI no: 10.1021/bi00214a003]
PubMed id 8260490
Note In the PDB file this reference is annotated as "TO BE PUBLISHED". The citation details given above were identified by an automated search of PubMed on title and author names, giving a percentage match of 88%.
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.
Secondary reference #1
Title Repair of DNA methylphosphotriesters through a metalloactivated cysteine nucleophile.
Authors L.C.Myers, M.P.Terranova, A.E.Ferentz, G.Wagner, G.L.Verdine.
Ref. Science, 1993, 261, 1164-1167. [DOI no: 10.1126/science.8395079]
PubMed id 8395079
Full text Abstract
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