4GK5

Crystal structure of human Rev3-Rev7-Rev1-Polkappa complex

Summary for 4GK5

• Entry DOI: 10.2210/pdb4gk5/pdb
• Related: 4GK0
• Descriptor: Mitotic spindle assembly checkpoint protein MAD2B, DNA polymerase zeta catalytic subunit, DNA repair protein REV1, ... (4 entities in total)
• Functional Keywords: translesion polymerases complex, four-helix bundle, beta-hairpin domain, anti-parallel sheets, translesion dna synthesis, polymerase switch, none, transferase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q9UI95 Q9UBT6; Nucleus (Potential): O60673; Nucleus (Probable): Q9UBZ9
• Total number of polymer chains: 7
• Total formula weight: 96818.99

Authors

Tao, J.,Min, X.,Wei, X. (deposition date: 2012-08-10, release date: 2013-03-13, Last modification date: 2023-11-08)

Primary citation

Xie, W.,Yang, X.,Xu, M.,Jiang, T.
Structural insights into the assembly of human translesion polymerase complexes
Protein Cell, 3:864-874, 2012

PubMed Abstract: In addition to DNA repair pathways, cells utilize translesion DNA synthesis (TLS) to bypass DNA lesions during replication. During TLS, Y-family DNA polymerase (Polη, Polκ, Polı and Rev1) inserts specific nucleotide opposite preferred DNA lesions, and then Polζ consisting of two subunits, Rev3 and Rev7, carries out primer extension. Here, we report the complex structures of Rev3-Rev7-Rev1(CTD) and Rev3-Rev7-Rev1(CTD)-Polκ(RIR). These two structures demonstrate that Rev1(CTD) contains separate binding sites for Polκ and Rev7. Our BIAcore experiments provide additional support for the notion that the interaction between Rev3 and Rev7 increases the affinity of Rev7 and Rev1. We also verified through FRET experiment that Rev1, Rev3, Rev7 and Polκ form a stable quaternary complex in vivo, thereby suggesting an efficient switching mechanism where the "inserter" polymerase can be immediately replaced by an "extender" polymerase within the same quaternary complex.

PubMed: 23143872
DOI: 10.1007/s13238-012-2102-x

Experimental method

X-RAY DIFFRACTION (3.21 Å)