1T6F

Crystal Structure of the Coiled-coil Dimerization Motif of Geminin

Summary for 1T6F

• Entry DOI: 10.2210/pdb1t6f/pdb
• Descriptor: Geminin (2 entities in total)
• Functional Keywords: coiled-coil, cell cycle
• Total number of polymer chains: 2
• Total formula weight: 8809.97

Authors

Thepaut, M.,Maiorano, D.,Guichou, J.-F.,Auge, M.-T.,Dumas, C.,Mechali, M.,Padilla, A. (deposition date: 2004-05-06, release date: 2004-07-27, Last modification date: 2023-08-23)

Primary citation

Thepaut, M.,Maiorano, D.,Guichou, J.-F.,Auge, M.-T.,Dumas, C.,Mechali, M.,Padilla, A.
Crystal Structure of the Coiled-coil Dimerization Motif of Geminin: Structural and Functional Insights on DNA Replication Regulation
J.Mol.Biol., 342:275-287, 2004

PubMed Abstract: We have determined the crystal structure of the coiled-coil domain of human geminin, a DNA synthesis inhibitor in higher eukaryotes. We show that a peptide encompassing the five heptad repeats of the geminin leucine zipper (LZ) domain is a dimeric parallel coiled coil characterized by a unique pattern of internal polar residues and a negatively charged surface that may target the basic domain of interacting partners. We show that the LZ domain itself is not sufficient to inhibit DNA synthesis but upstream and downstream residues are required. Analysis of a functional form of geminin by density sedimentation indicates an oligomeric structure. X-ray solution scattering experiments performed on a non-functional form of geminin having upstream basic residues and the LZ domain show a tetramer structure. Altogether, these results give a consistent identification and mapping of geminin interacting regions onto structurally important domains. They also suggest that oligomerization properties of geminin may be implicated in its inhibitory activity of DNA synthesis.

PubMed: 15313623
DOI: 10.1016/j.jmb.2004.06.065

Experimental method

X-RAY DIFFRACTION (1.47 Å)