1bnk

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1bnk, resolution 2.7Å

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HUMAN 3-METHYLADENINE DNA GLYCOSYLASE COMPLEXED TO DNA

Contents

Overview

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.

Disease

Known disease associated with this structure: Opitz G syndrome, type I OMIM:[300552]

About this Structure

1BNK is a Single protein structure of sequence from Homo sapiens. Active as DNA-3-methyladenine glycosylase II, with EC number 3.2.2.21 Full crystallographic information is available from OCA.

Reference

Crystal structure of a human alkylbase-DNA repair enzyme complexed to DNA: mechanisms for nucleotide flipping and base excision., Lau AY, Scharer OD, Samson L, Verdine GL, Ellenberger T, Cell. 1998 Oct 16;95(2):249-58. PMID:9790531

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