Structural highlights
Function
[RAD50_PYRFU] Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity. Rad50 provides an ATP-dependent control of Mre11 by unwinding and/or repositioning DNA ends into the Mre11 active site.[HAMAP-Rule:MF_00449]
Publication Abstract from PubMed
The Rad50-Mre11 nuclease complex plays a vital role in DNA repair in all domains of life. It recognizes and processes DNA double-strand breaks. Rad50 proteins fold into an extended structure with a ~ 20-60 nm long coiled coil connecting a globular ABC ATPase domain with a zinc hook dimerization domain. A published structure of an archaeal Rad50 zinc hook shows coiled coils pointing away from each other. Here we present the crystal structure of an alternate conformation displaying co-aligned coiled coils. Archaeal Rad50 may thus switch between rod-shaped and ring-like conformations as recently proposed for a bacterial homolog. This article is protected by copyright. All rights reserved.
A rod conformation of the Pyrococcus furiosus Rad50 coiled coil.,Soh YM, Basquin J, Gruber S Proteins. 2020 Sep 2. doi: 10.1002/prot.26005. PMID:32875643[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Soh YM, Basquin J, Gruber S. A rod conformation of the Pyrococcus furiosus Rad50 coiled coil. Proteins. 2020 Sep 2. doi: 10.1002/prot.26005. PMID:32875643 doi:http://dx.doi.org/10.1002/prot.26005
