5M1X: Crystal Structure Of S. Cerevisiae Rfa1 N-ob Domain Mutant (k45e)

Citation:
Abstract
The Mre11-Rad50-Xrs2 (MRX) complex is related to SMC complexes that form rings capable of holding two distinct DNA strands together. MRX functions at stalled replication forks and double-strand breaks (DSBs). A mutation in the N-terminal OB fold of the 70 kDa subunit of yeast replication protein A, rfa1-t11, abrogates MRX recruitment to both types of DNA damage. The rfa1 mutation is functionally epistatic with loss of any of the MRX subunits for survival of replication fork stress or DSB recovery, although it does not compromise end-resection. High-resolution imaging shows that either the rfa1-t11 or the rad50Delta mutation lets stalled replication forks collapse and allows the separation not only of opposing ends but of sister chromatids at breaks. Given that cohesin loss does not provoke visible sister separation as long as the RPA-MRX contacts are intact, we conclude that MRX also serves as a structural linchpin holding sister chromatids together at breaks.
PDB ID: 5M1XDownload
MMDB ID: 145497
PDB Deposition Date: 2016/10/11
Updated in MMDB: 2016/12
Experimental Method:
x-ray diffraction
Resolution: 1.8  Å
Source Organism:
Similar Structures:
Biological Unit for 5M1X: monomeric; determined by author
Molecular Components in 5M1X
Label Count Molecule
Protein (1 molecule)
1
Replication Factor a Protein 1(Gene symbol: RFA1)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

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