3V62: Structure Of The S. Cerevisiae Srs2 C-terminal Domain In Complex With Pcna Conjugated To Sumo On Lysine 164

Ubiquitin (Ub) and ubiquitin-like (Ubl) modifiers such as SUMO (also known as Smt3 in Saccharomyces cerevisiae) mediate signal transduction through post-translational modification of substrate proteins in pathways that control differentiation, apoptosis and the cell cycle, and responses to stress such as the DNA damage response. In yeast, the proliferating cell nuclear antigen PCNA (also known as Pol30) is modified by ubiquitin in response to DNA damage and by SUMO during S phase. Whereas Ub-PCNA can signal for recruitment of translesion DNA polymerases, SUMO-PCNA signals for recruitment of the anti-recombinogenic DNA helicase Srs2. It remains unclear how receptors such as Srs2 specifically recognize substrates after conjugation to Ub and Ubls. Here we show, through structural, biochemical and functional studies, that the Srs2 carboxy-terminal domain harbours tandem receptor motifs that interact independently with PCNA and SUMO and that both motifs are required to recognize SUMO-PCNA specifically. The mechanism presented is pertinent to understanding how other receptors specifically recognize Ub- and Ubl-modified substrates to facilitate signal transduction.
PDB ID: 3V62Download
MMDB ID: 97646
PDB Deposition Date: 2011/12/18
Updated in MMDB: 2017/11
Experimental Method:
x-ray diffraction
Resolution: 2.9  Å
Source Organism:
Similar Structures:
Biological Unit for 3V62: trimeric; determined by author and by software (PISA)
Molecular Components in 3V62
Label Count Molecule
Proteins (3 molecules)
Ubiquitin-like Protein Smt3(Gene symbol: SMT3)
Molecule annotation
Proliferating Cell Nuclear Antigen(Gene symbol: POL30)
Molecule annotation
Atp-dependent DNA Helicase Srs2(Gene symbol: SRS2)
Molecule annotation
Chemicals (5 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB