beta-strand (B) domain of GINS complex protein Sld5
Sld5 is a component of the GINS (named from the Japanese go-ichi-ni-san, meaning 5-1-2-3 for the Sld5, Psf1, Psf2, and Psf3 subunits) tetrameric protein complex, within which Sld5 interacts with Psf1 via its N-terminal A-domain, and with Psf2 through a combination of the A and B domains. In Drosophila, Sld5 is required for normal cell cycle progression and the maintenance of genomic integrity. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits Sld5, Psf1, Psf2 and Psf3 are homologous, and homologs are also found in archaea; the complex is not found in bacteria. Each subunit of the complex consists of two domains called the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3. This model represents the B-domain of GINS subunit Sld5.
Structure:2Q9Q, human GINS subunit Sld5 interface with other subunits in the heterotetramer; contacts at 4A - View structure with Cn3D
Comment:the GINS complex contains four subunits: Sld5, Psf1, Psf2, and Psf3; it functions as a tight heterotetrameric complex in which major interactions are mediated through helix-helix interactions that amplify the helix-bundle-like structure of each individual subunit
Jiyao W et al.(2023). "The conserved domain database in 2023.",