1mpg

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[[Image:1mpg.gif|left|200px]]
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{{STRUCTURE_1mpg| PDB=1mpg | SCENE= }}
{{STRUCTURE_1mpg| PDB=1mpg | SCENE= }}
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'''3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI'''
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===3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8706136 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8706136}}
==About this Structure==
==About this Structure==
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[[Category: Hydrolase]]
[[Category: Hydrolase]]
[[Category: Methylation]]
[[Category: Methylation]]
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Revision as of 21:41, 2 July 2008

Template:STRUCTURE 1mpg

3-METHYLADENINE DNA GLYCOSYLASE II FROM ESCHERICHIA COLI

Template:ABSTRACT PUBMED 8706136

About this Structure

1MPG is a Single protein structure of sequence from Escherichia coli. 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

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