6J0V

Crystal Structure of Yeast Rtt107

Summary for 6J0V

• Entry DOI: 10.2210/pdb6j0v/pdb
• Descriptor: Regulator of Ty1 transposition protein 107 (2 entities in total)
• Functional Keywords: brct domain, mitosis, protein interaction, protein binding
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
• Total number of polymer chains: 2
• Total formula weight: 118719.94

Authors

Wan, B.,Wu, J.,Lei, M. (deposition date: 2018-12-27, release date: 2019-08-14, Last modification date: 2024-03-27)

Primary citation

Wan, B.,Wu, J.,Meng, X.,Lei, M.,Zhao, X.
Molecular Basis for Control of Diverse Genome Stability Factors by the Multi-BRCT Scaffold Rtt107.
Mol.Cell, 75:238-251.e5, 2019

PubMed Abstract: BRCT domains support myriad protein-protein interactions involved in genome maintenance. Although di-BRCT recognition of phospho-proteins is well known to support the genotoxic response, whether multi-BRCT domains can acquire distinct structures and functions is unclear. Here we present the tetra-BRCT structures from the conserved yeast protein Rtt107 in free and ligand-bound forms. The four BRCT repeats fold into a tetrahedral structure that recognizes unmodified ligands using a bi-partite mechanism, suggesting repeat origami enabling function acquisition. Functional studies show that Rtt107 binding of partner proteins of diverse activities promotes genome replication and stability in both distinct and concerted manners. A unified theme is that tetra- and di-BRCT domains of Rtt107 collaborate to recruit partner proteins to chromatin. Our work thus illustrates how a master regulator uses two types of BRCT domains to recognize distinct genome factors and direct them to chromatin for constitutive genome protection.

PubMed: 31348879
DOI: 10.1016/j.molcel.2019.05.035

Experimental method

X-RAY DIFFRACTION (2.314 Å)