1ee8

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spinqualitylabelsall models 1ee8, resolution 1.9Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF MUTM (FPG) PROTEIN FROM THERMUS THERMOPHILUS HB8

Overview

The MutM [formamidopyrimidine DNA glycosylase (Fpg)] protein is a, trifunctional DNA base excision repair enzyme that removes a wide range of, oxidatively damaged bases (N-glycosylase activity) and cleaves both the, 3'- and 5'-phosphodiester bonds of the resulting apurinic/apyrimidinic, site (AP lyase activity). The crystal structure of MutM from an extreme, thermophile, Thermus thermophilus HB8, was determined at 1.9 A resolution, with multiwavelength anomalous diffraction phasing using the intrinsic, Zn(2+) ion of the zinc finger. MutM is composed of two distinct and novel, domains connected by a flexible hinge. There is a large, electrostatically, positive cleft lined by highly conserved residues between the domains. On, the basis of the three-dimensional structure and taking account of, previous biochemical experiments, we propose a DNA-binding mode and, reaction mechanism for MutM. The locations of the putative catalytic, residues and the two DNA-binding motifs (the zinc finger and the, helix-two-turns-helix motifs) suggest that the oxidized base is flipped, out from double-stranded DNA in the binding mode and excised by a, catalytic mechanism similar to that of bifunctional base excision repair, enzymes.

About this Structure

1EE8 is a Single protein structure of sequence from Thermus thermophilus with ZN as ligand. Full crystallographic information is available from OCA.

Reference

Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8., Sugahara M, Mikawa T, Kumasaka T, Yamamoto M, Kato R, Fukuyama K, Inoue Y, Kuramitsu S, EMBO J. 2000 Aug 1;19(15):3857-69. PMID:10921868

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