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5VZM

Solution NMR structure of human Rev1 (932-1039) in complex with ubiquitin

Summary for 5VZM
Entry DOI10.2210/pdb5vzm/pdb
NMR InformationBMRB: 30300
DescriptorUbiquitin, DNA repair protein REV1 (2 entities in total)
Functional Keywordstranslesion dna synthesis, dna repair, dna replication, rev1, ubiquitin, pcna, protein binding
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains2
Total formula weight20562.18
Authors
Cui, G.,Botuyan, M.V.,Mer, G. (deposition date: 2017-05-29, release date: 2018-05-23, Last modification date: 2024-11-13)
Primary citationCui, G.,Botuyan, M.V.,Mer, G.
Structural Basis for the Interaction of Mutasome Assembly Factor REV1 with Ubiquitin.
J. Mol. Biol., 430:2042-2050, 2018
Cited by
PubMed Abstract: REV1 is an evolutionarily conserved translesion synthesis (TLS) DNA polymerase and an assembly factor key for the recruitment of other TLS polymerases to DNA damage sites. REV1-mediated recognition of ubiquitin in the proliferative cell nuclear antigen is thought to be the trigger for TLS activation. Here we report the solution NMR structure of a 108-residue fragment of human REV1 encompassing the two putative ubiquitin-binding motifs UBM1 and UBM2 in complex with ubiquitin. While in mammals UBM1 and UBM2 are both required for optimal association of REV1 with replication factories after DNA damage, we show that only REV1 UBM2 binds ubiquitin. Structure-guided mutagenesis in Saccharomyces cerevisiae further highlights the importance of UBM2 for REV1-mediated mutagenesis and DNA damage tolerance.
PubMed: 29778604
DOI: 10.1016/j.jmb.2018.05.017
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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