5GOX

Eukaryotic Rad50 Functions as A Rod-shaped Dimer

Summary for 5GOX

• Entry DOI: 10.2210/pdb5gox/pdb
• Descriptor: DNA repair protein RAD50, GLYCEROL, ZINC ION, ... (4 entities in total)
• Functional Keywords: dna repair, hydrolase
• Biological source: Homo sapiens (Human)
• Cellular location: Nucleus : Q92878
• Total number of polymer chains: 2
• Total formula weight: 44094.05

Authors

Park, Y.B.,Hohl, M.,Padjasek, M.,Jeong, E.,Jin, K.S.,Krezel, A.,Petrini, J.H.J.,Cho, Y. (deposition date: 2016-07-30, release date: 2017-02-01, Last modification date: 2024-11-06)

Primary citation

Park, Y.B.,Hohl, M.,Padjasek, M.,Jeong, E.,Jin, K.S.,Krezel, A.,Petrini, J.H.J.,Cho, Y.
Eukaryotic Rad50 functions as a rod-shaped dimer
Nat. Struct. Mol. Biol., 24:248-257, 2017

PubMed Abstract: The Rad50 hook interface is crucial for assembly and various functions of the Mre11 complex. Previous analyses suggested that Rad50 molecules interact within (intracomplex) or between (intercomplex) dimeric complexes. In this study, we determined the structure of the human Rad50 hook and coiled-coil domains. The data suggest that the predominant structure is the intracomplex, in which the two parallel coiled coils proximal to the hook form a rod shape, and that a novel interface within the coiled-coil domains of Rad50 stabilizes the interaction of Rad50 protomers in the dimeric assembly. In yeast, removal of the coiled-coil interface compromised Tel1 activation without affecting DNA repair, while simultaneous disruption of that interface and the hook phenocopied a null mutation. The results demonstrate that the hook and coiled-coil interfaces coordinately promote intracomplex assembly and define the intracomplex as the functional form of the Mre11 complex.

PubMed: 28134932
DOI: 10.1038/nsmb.3369

Experimental method

X-RAY DIFFRACTION (2.405 Å)