5MQI

Crystal structure of the N-terminal domain of human Timeless

Summary for 5MQI

• Entry DOI: 10.2210/pdb5mqi/pdb
• Descriptor: Protein timeless homolog,Protein timeless homolog, SULFATE ION (3 entities in total)
• Functional Keywords: dna replication, genomic stability, replication
• Biological source: Homo sapiens (Human); More
• Cellular location: Nucleus : Q9UNS1
• Total number of polymer chains: 1
• Total formula weight: 44243.05

Authors

Holzer, S.,Kilkenny, M.L.,Pellegrini, L. (deposition date: 2016-12-20, release date: 2017-03-08, Last modification date: 2024-05-08)

Primary citation

Holzer, S.,Degliesposti, G.,Kilkenny, M.L.,Maslen, S.L.,Matak-Vinkovic, D.,Skehel, M.,Pellegrini, L.
Crystal structure of the N-terminal domain of human Timeless and its interaction with Tipin.
Nucleic Acids Res., 45:5555-5563, 2017

PubMed Abstract: Human Timeless is involved in replication fork stabilization, S-phase checkpoint activation and establishment of sister chromatid cohesion. In the cell, Timeless forms a constitutive heterodimeric complex with Tipin. Here we present the 1.85 Å crystal structure of a large N-terminal segment of human Timeless, spanning amino acids 1-463, and we show that this region of human Timeless harbours a partial binding site for Tipin. Furthermore, we identify minimal regions of the two proteins that are required for the formation of a stable Timeless-Tipin complex and provide evidence that the Timeless-Tipin interaction is based on a composite binding interface comprising different domains of Timeless.

PubMed: 28334766
DOI: 10.1093/nar/gkx139

Experimental method

X-RAY DIFFRACTION (1.847 Å)