1F4R

CRYSTAL STRUCTURE OF THE HUMAN AAG DNA REPAIR GLYCOSYLASE COMPLEXED WITH 1,N6-ETHENOADENINE-DNA

Summary for 1F4R

• Entry DOI: 10.2210/pdb1f4r/pdb
• Related: 1BNK 1EWN
• Descriptor: DNA (5'-D(*GP*AP*CP*AP*TP*GP*(EDA)P*TP*TP*GP*CP*CP*T)-3'), DNA (5'-D(*GP*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3'), 3-METHYL-ADENINE DNA GLYCOSYLASE, ... (5 entities in total)
• Functional Keywords: protein-dna complex, hydrolase-dna complex, hydrolase/dna
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 32318.14

Authors

Lau, A.Y.,Wyatt, M.D.,Glassner, B.J.,Samson, L.D.,Ellenberger, T. (deposition date: 2000-06-08, release date: 2000-12-11, Last modification date: 2024-02-07)

Primary citation

Lau, A.Y.,Wyatt, M.D.,Glassner, B.J.,Samson, L.D.,Ellenberger, T.
Molecular basis for discriminating between normal and damaged bases by the human alkyladenine glycosylase, AAG.
Proc.Natl.Acad.Sci.USA, 97:13573-13578, 2000

PubMed Abstract: The human 3-methyladenine DNA glycosylase [alkyladenine DNA glycosylase (AAG)] catalyzes the first step of base excision repair by cleaving damaged bases from DNA. Unlike other DNA glycosylases that are specific for a particular type of damaged base, AAG excises a chemically diverse selection of substrate bases damaged by alkylation or deamination. The 2.1-A crystal structure of AAG complexed to DNA containing 1,N(6)-ethenoadenine suggests how modified bases can be distinguished from normal DNA bases in the enzyme active site. Mutational analyses of residues contacting the alkylated base in the crystal structures suggest that the shape of the damaged base, its hydrogen-bonding characteristics, and its aromaticity all contribute to the selective recognition of damage by AAG.

PubMed: 11106395
DOI: 10.1073/pnas.97.25.13573

Experimental method

X-RAY DIFFRACTION (2.4 Å)