1BNK

HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA

Summary for 1BNK

• Entry DOI: 10.2210/pdb1bnk/pdb
• Descriptor: DNA (5'-D(*GP*AP*CP*AP*TP*GP*YRRP*TP*TP*GP*CP*CP*T)-3'), DNA (5'-D(*GP*GP*CP*AP*AP*TP*CP*AP*TP*GP*TP*CP*A)-3'), PROTEIN (3-METHYLADENINE DNA GLYCOSYLASE), ... (4 entities in total)
• Functional Keywords: dna repair, dna glycosylase, hydrolase-dna complex, hydrolase/dna
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 3
• Total formula weight: 31859.74

Authors

Lau, A.Y.,Schaerer, O.D.,Samson, L.,Verdine, G.L.,Ellenberger, T. (deposition date: 1998-07-29, release date: 1998-10-21, Last modification date: 2023-12-27)

Primary citation

Lau, A.Y.,Scharer, O.D.,Samson, L.,Verdine, G.L.,Ellenberger, T.
Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision.
Cell(Cambridge,Mass.), 95:249-258, 1998

PubMed Abstract: DNA N-glycosylases are base excision-repair proteins that locate and cleave damaged bases from DNA as the first step in restoring the genetic blueprint. The human enzyme 3-methyladenine DNA glycosylase removes a diverse group of damaged bases from DNA, including cytotoxic and mutagenic alkylation adducts of purines. We report the crystal structure of human 3-methyladenine DNA glycosylase complexed to a mechanism-based pyrrolidine inhibitor. The enzyme has intercalated into the minor groove of DNA, causing the abasic pyrrolidine nucleotide to flip into the enzyme active site, where a bound water is poised for nucleophilic attack. The structure shows an elegant means of exposing a nucleotide for base excision as well as a network of residues that could catalyze the in-line displacement of a damaged base from the phosphodeoxyribose backbone.

PubMed: 9790531
DOI: 10.1016/S0092-8674(00)81755-9

Experimental method

X-RAY DIFFRACTION (2.7 Å)