1mpg
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(New page: 200px<br /><applet load="1mpg" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mpg, resolution 1.80Å" /> '''3-METHYLADENINE DNA ...)
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Revision as of 19:29, 20 November 2007
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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 GOL 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 Tue Nov 20 21:36:32 2007
