4YKE

Crystal structure of eukaryotic Mre11 catalytic domain from Chaetomium thermophilum

Summary for 4YKE

• Entry DOI: 10.2210/pdb4yke/pdb
• Descriptor: Mre11, MANGANESE (II) ION (3 entities in total)
• Functional Keywords: nuclease, hydrolase, catalytic domain, nuclear proteins, protein binding
• Biological source: Chaetomium thermophilum
• Total number of polymer chains: 2
• Total formula weight: 126188.06

Authors

Seifert, F.U.,Lammens, K.,Hopfner, K.-P. (deposition date: 2015-03-04, release date: 2015-06-03, Last modification date: 2024-01-10)

Primary citation

Seifert, F.U.,Lammens, K.,Hopfner, K.P.
Structure of the catalytic domain of Mre11 from Chaetomium thermophilum.
Acta Crystallogr.,Sect.F, 71:752-757, 2015

PubMed Abstract: Together with the Rad50 ATPase, the Mre11 nuclease forms an evolutionarily conserved protein complex that plays a central role in the repair of DNA double-strand breaks (DSBs). Mre11-Rad50 detects and processes DNA ends, and has functions in the tethering as well as the signalling of DSBs. The Mre11 dimer can bind one or two DNA ends or hairpins, and processes DNA endonucleolytically as well as exonucleolytically in the 3'-to-5' direction. Here, the crystal structure of the Mre11 catalytic domain dimer from Chaetomium thermophilum (CtMre11(CD)) is reported. CtMre11(CD) crystals diffracted to 2.8 Å resolution and revealed previously undefined features within the dimer interface, in particular fully ordered eukaryote-specific insertion loops that considerably expand the dimer interface. Furthermore, comparison with other eukaryotic Mre11 structures reveals differences in the conformations of the dimer and the capping domain. In summary, the results reported here provide new insights into the architecture of the eukaryotic Mre11 dimer.

PubMed: 26057807
DOI: 10.1107/S2053230X15007566

Experimental method

X-RAY DIFFRACTION (2.783 Å)