1MPG

3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI

Summary for 1MPG

• Entry DOI: 10.2210/pdb1mpg/pdb
• Descriptor: 3-METHYLADENINE DNA GLYCOSYLASE II, GLYCEROL (3 entities in total)
• Functional Keywords: dna glycosylase, dna repair, base excision, methylation, alka, hydrolase
• Biological source: Escherichia coli
• Total number of polymer chains: 2
• Total formula weight: 63034.66

Authors

Labahn, J.,Schaerer, O.D.,Long, A.,Ezaz-Nikpay, K.,Verdine, G.L.,Ellenberger, T.E. (deposition date: 1997-10-28, release date: 1998-01-28, Last modification date: 2024-02-14)

Primary citation

Labahn, J.,Scharer, O.D.,Long, A.,Ezaz-Nikpay, K.,Verdine, G.L.,Ellenberger, T.E.
Structural basis for the excision repair of alkylation-damaged DNA.
Cell(Cambridge,Mass.), 86:321-329, 1996

PubMed Abstract: Base-excision DNA repair proteins that target alkylation damage act on a variety of seemingly dissimilar adducts, yet fail to recognize other closely related lesions. The 1.8 A crystal structure of the monofunctional DNA glycosylase AlkA (E. coli 3-methyladenine-DNA glycosylase II) reveals a large hydrophobic cleft unusually rich in aromatic residues. An Asp residue projecting into this cleft is essential for catalysis, and it governs binding specificity for mechanism-based inhibitors. We propose that AlkA recognizes electron-deficient methylated bases through pi-donor/acceptor interactions involving the electron-rich aromatic cleft. Remarkably, AlkA is similar in fold and active site location to the bifunctional glycosylase/lyase endonuclease III, suggesting the two may employ fundamentally related mechanisms for base excision.

PubMed: 8706136
DOI: 10.1016/S0092-8674(00)80103-8

Experimental method

X-RAY DIFFRACTION (1.8 Å)