1EE8

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

Summary for 1EE8

• Entry DOI: 10.2210/pdb1ee8/pdb
• Descriptor: MUTM (FPG) PROTEIN, ZINC ION (3 entities in total)
• Functional Keywords: beta sandwich, zinc finger, helix two-turns helix, riken structural genomics/proteomics initiative, rsgi, structural genomics, dna binding protein
• Biological source: Thermus thermophilus
• Total number of polymer chains: 2
• Total formula weight: 59797.43

Authors

Sugahara, M.,Mikawa, T.,Kumasaka, T.,Yamamoto, M.,Kato, R.,Fukuyama, K.,Inoue, Y.,Kuramitsu, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2000-01-31, release date: 2001-01-31, Last modification date: 2024-02-07)

Primary citation

Sugahara, M.,Mikawa, T.,Kumasaka, T.,Yamamoto, M.,Kato, R.,Fukuyama, K.,Inoue, Y.,Kuramitsu, S.
Crystal structure of a repair enzyme of oxidatively damaged DNA, MutM (Fpg), from an extreme thermophile, Thermus thermophilus HB8.
EMBO J., 19:3857-3869, 2000

PubMed Abstract: 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.

PubMed: 10921868
DOI: 10.1093/emboj/19.15.3857

Experimental method

X-RAY DIFFRACTION (1.9 Å)