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6J0W

Crystal Structure of Yeast Rtt107 and Nse6

Summary for 6J0W
Entry DOI10.2210/pdb6j0w/pdb
Related6J0V
DescriptorRegulator of Ty1 transposition protein 107, Peptide from DNA repair protein KRE29 (3 entities in total)
Functional Keywordsbrct domain, mitosis, protein interaction, protein binding
Biological sourceSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
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Total number of polymer chains4
Total formula weight125042.50
Authors
Wan, B.,Wu, J.,Lei, M. (deposition date: 2018-12-27, release date: 2019-08-14, Last modification date: 2023-11-22)
Primary citationWan, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.4 Å)
Structure validation

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數據於2024-11-06公開中

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