Research article
Atomic structures and functional implications of the archaeal RecQ-like helicase Hjm
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* Corresponding author: Kosuke Morikawa morikako@protein.osaka-u.ac.jp
1 The Takara Bio Endowed Division, Institute for Protein Research, Osaka University, Open Laboratories of Advanced Bioscience and Biotechnology (OLABB), 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan
2 Department of Genetic Resources Technology, Faculty of Agriculture, Kyushu University, 6-10-1 Hakozaki, Fukuoka-shi, Fukuoka, 812-8581, Japan
3 Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan
4 Department of Bioscience, Nagahama Institute of Bioscience and Technology, 1266 Tamura, Nagahama 526-0829, Japan
5 Laboratory of Protein Synthesis and Expression, Institute for Protein Research, 3-2 Yamadaoka, Suita, Osaka 565-0874, Japan
6 BIRD, JST, Japan
7 Research & Develop center, Terumo Corporation, 1500, Inokuchi, Nakai-machi, Ashigarakami-gun, Kanagawa, 259-0151, Japan
8 Univ. Paris-Sud, Institut de Génétique et Microbiologie, CNRS, UMR 8621, F-91405 Orsay Cedex, France
BMC Structural Biology 2009, 9:2 doi:10.1186/1472-6807-9-2
Published: 22 January 2009Additional files
Additional file 1:
Multiple sequence alignment. Hjm helicases and the homologues of Pyrococcus furiosus (Euryarchaeota, Hel_Pfu, O73946|HELS_PYRFU), Archaeoglobus fulgidus (Euryarchaeota, Hel_Afu, NC_000917.1), Methanococcus vannielii (Euryarchaeota, Hel_Mva, A2UUA3|A2UUA3_METVA), Sulfolobus solfataricus (Crenarchaeote, Hel_Sso, Q97VY9|HELS_SULSO), and Methanopyrus kandleri (Euryarchaeota, Hel_Mka, Q8TGZ1|Q8TGZ1_METKA), and DNA polymerase Θ s and the homologues of Homo sapiens (human, PolQ_Has, Q96SE4|Q96SE4_HUMAN), Mus musculus (mouse, PolQ_Mmu, Q80XB7|Q80XB7_MOUSE), Aspergillus oryzae (fungus, PolQ_Aor, Q2UKG1|Q2UKG1_ASPOR), Aedes aegypti (mosquito, PolQ_Aae, Q178I3|Q178I3_AEDAE), and Trypanosoma brucei (protista, PolQ_Tbr, Q57YX8|Q57YX8_9TRYP) are aligned (in parentheses are the organism common name, name in the alignment, and UniProt or Refseq code). The presented sequences were selected from a total of 341 sequences as the representatives of clusters. The conservative Cys residues among the DNA polymerases are indicated by + (conserved among the shown sequences: Cys322 and Cys477) or # (conserved except for protista: Cys232, Cys483, Cys629, Cys651, and Cys289) below the alignment. Amino acid residues are colored according to their characteristics (aromatic, cyan; hydrophobic, green; basic, brown; ambivalent, orange). Secondary structural elements are indicated on the top of the sequences. DNA binding residues in the A. fulgidus hel308-DNA complex are depicted by triangles. Putative disulfide bond-forming residues in the human PolΘ helicase domain model are colored yellow-. The figure was prepared with ClustalX.
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Additional file 2:
Homology model of the human DNA polymerase Θ helicase domain. The model was built using the program MOE (Ryoka Systems Inc.)
Format: PDB Size: 484KB Download file