1k82

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Revision as of 16:48, 20 November 2007

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spinqualitylabelsall models 1k82, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal structure of E.coli formamidopyrimidine-DNA glycosylase (Fpg) covalently trapped with DNA

Overview

Formamidopyrimidine-DNA glycosylase (Fpg) is a DNA repair enzyme that, excises oxidized purines from damaged DNA. The Schiff base intermediate, formed during this reaction between Escherichia coli Fpg and DNA was, trapped by reduction with sodium borohydride, and the structure of the, resulting covalently cross-linked complex was determined at a 2.1-A, resolution. Fpg is a bilobal protein with a wide, positively charged, DNA-binding groove. It possesses a conserved zinc finger and a helix-two, turn-helix motif that participate in DNA binding. The absolutely conserved, residues Lys-56, His-70, Asn-168, and Arg-258 form hydrogen bonds to the, phosphodiester backbone of DNA, which is sharply kinked at the lesion, site. Residues Met-73, Arg-109, and Phe-110 are inserted into the DNA, helix, filling the void created by nucleotide eversion. A deep hydrophobic, pocket in the active site is positioned to accommodate an everted base., Structural analysis of the Fpg-DNA complex reveals essential features of, damage recognition and the catalytic mechanism of Fpg.

About this Structure

1K82 is a Single protein structure of sequence from Escherichia coli with ZN as ligand. Active as DNA-formamidopyrimidine glycosylase, with EC number 3.2.2.23 Full crystallographic information is available from OCA.

Reference

Structure of formamidopyrimidine-DNA glycosylase covalently complexed to DNA., Gilboa R, Zharkov DO, Golan G, Fernandes AS, Gerchman SE, Matz E, Kycia JH, Grollman AP, Shoham G, J Biol Chem. 2002 May 31;277(22):19811-6. Epub 2002 Mar 23. PMID:11912217

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