Crystal structure of the human GINS complex
- Jung Min Choi1,2,3,
- Hye Seong Lim1,2,3,
- Jeong Joo Kim1,2,
- Ok-Kyu Song2, and
- Yunje Cho1,2,4
- 1 National Creative Initiatives for Structural Biology, Pohang University of Science and Technology, Pohang, Kyung Book 790-784, South Korea;
- 2 Department of Life Science, Pohang University of Science and Technology, Pohang, Kyung Book 790-784, South Korea
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↵3 These authors contributed equally to this work.
Abstract
The GINS complex mediates the assembly of the MCM2–7 (minichromosome maintenance) complex with proteins in a replisome progression complex. The eukaryotic GINS complex is composed of Sld5, Psf1, Psf2, and Psf3, which must be assembled for cell proliferation. We determined the crystal structure of the human GINS complex: GINS forms an elliptical shape with a small central channel. The structures of Sld5 and Psf2 resemble those of Psf1 and Psf3, respectively. In addition, the N-terminal and C-terminal domains of Sld5/Psf1 are permuted in Psf2/Psf3, which suggests that the four proteins have evolved from a common ancestor. Using a structure-based mutational analysis, we identified the functionally critical surface regions of the GINS complex.
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Footnotes
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↵4 Corresponding author.
↵4 EMAIL yunje{at}postech.ac.kr; FAX 82-54-279-8111.
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Supplemental material is available at http://www.genesdev.org.
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Article is online at http://www.genesdev.org/cgi/doi/10.1101/gad.1548107
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- Received March 2, 2007.
- Accepted April 19, 2007.
- Copyright © 2007, Cold Spring Harbor Laboratory Press
