1mpg
From Proteopedia
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3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI
Overview
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.
About this Structure
1MPG is a Single protein structure of sequence from Escherichia coli with as ligand. Active as DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 Full crystallographic information is available from OCA.
Reference
Structural basis for the excision repair of alkylation-damaged DNA., Labahn J, Scharer OD, Long A, Ezaz-Nikpay K, Verdine GL, Ellenberger TE, Cell. 1996 Jul 26;86(2):321-9. PMID:8706136
Page seeded by OCA on Thu Feb 21 13:57:39 2008
