Open Access Research article

Architectures of archaeal GINS complexes, essential DNA replication initiation factors

Takuji Oyama15, Sonoko Ishino2, Seiji Fujino2, Hiromi Ogino2, Tsuyoshi Shirai35, Kouta Mayanagi45, Mihoko Saito3, Naoko Nagasawa1, Yoshizumi Ishino25 and Kosuke Morikawa1*

Author Affiliations

1 Laboratory of Protein Organic Chemistry, 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 Bioscience & Biotechnology, Faculty of Agriculture and Graduate School of Bioscience & Bioenvironmental Sciences, Kyushu University, 6-10-1 Hakozaki, Higashi-ku, Fukuoka-shi, Fukuoka, 812-8581, Japan

3 Department of Bioscience, Nagahama Institute of Bioscience and Technology, 1266 Tamura, Nagahama 526-0829, Japan

4 Division of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Maidashi 3-1-1, Higashi-ku, Fukuoka 812-8582, Japan

5 BIRD, JST, Japan

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BMC Biology 2011, 9:28  doi:10.1186/1741-7007-9-28

Published: 28 April 2011

Additional files

Additional file 1:

Structure comparison of the TkoGINS B domains with the C-terminal domain of the primase small subunit (PriS-CTD) from Sulfolobus solfataricus (PDB code 1ZT2 chain A). (A) Stereo view of the superimposed structures. TkoGins51 B domain is colored green, TkoGins23 B domain is cyan, and Pris-CTD is pink. The Gins23 B domain superimposed on the Gins51 B domain with an RMSD of 0.81 Å, using the corresponding 38 Cα atoms, and the PriS-CTD superimposed on the Gins51 B domain with an RMSD of 0.85 Å, using 31 Cα atoms. (B) Structure-based sequence alignment.

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Additional file 2:

Crystal packing interactions. (A) Overall view of the crystal packing. Each tetramer contacts the surrounding four tetramers in the crystal with the same interaction mode. (B) Close-up view of the packing interaction boxed in (A). A Gins51 B domain contacts a Gins23 B domain in the neighboring tetramer.

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Additional file 3:

Detailed subunit contacts in the GINS complexes. Close-up views of the subunit contacts between Gins51 and Gins23 in TkoGINS (A), Sld5 and Psf2 in human GINS (B), and Psf1 and Psf3 in human GINS(C) are shown by stereo pairs. Residues involved in the contacts are depicted with stick models. (D) to (F) Schematic representations of the contacts.

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