2E9X
The crystal structure of human GINS core complex
Summary for 2E9X
Entry DOI | 10.2210/pdb2e9x/pdb |
Descriptor | DNA replication complex GINS protein PSF1, DNA replication complex GINS protein PSF2, GINS complex subunit 3, ... (6 entities in total) |
Functional Keywords | gins complex, eukaryotic dna replication, replication |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus : Q14691 Q9Y248 Q9BRX5 Cytoplasm : Q9BRT9 |
Total number of polymer chains | 8 |
Total formula weight | 180361.57 |
Authors | Kamada, K.,Hanaoka, F. (deposition date: 2007-01-27, release date: 2007-04-10, Last modification date: 2024-03-13) |
Primary citation | Kamada, K.,Kubota, Y.,Arata, T.,Shindo, Y.,Hanaoka, F. Structure of the human GINS complex and its assembly and functional interface in replication initiation Nat.Struct.Mol.Biol., 14:388-396, 2007 Cited by PubMed Abstract: The eukaryotic GINS complex is essential for the establishment of DNA replication forks and replisome progression. We report the crystal structure of the human GINS complex. The heterotetrameric complex adopts a pseudo symmetrical layered structure comprising two heterodimers, creating four subunit-subunit interfaces. The subunit structures of the heterodimers consist of two alternating domains. The C-terminal domains of the Sld5 and Psf1 subunits are connected by linker regions to the core complex, and the C-terminal domain of Sld5 is important for core complex assembly. In contrast, the C-terminal domain of Psf1 does not contribute to the stability of the complex but is crucial for chromatin binding and replication activity. These data suggest that the core complex ensures a stable platform for the C-terminal domain of Psf1 to act as a key interaction interface for other proteins in the replication-initiation process. PubMed: 17417653DOI: 10.1038/nsmb1231 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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