4gk0 | pdb_00004gk0

Crystal structure of human Rev3-Rev7-Rev1 complex

spinqualitylabelsall models 4gk0, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4gk0 is a 6 chain structure with sequence from Clostridium acetobutylicum and Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 4gk5 Gene: MAD2L2, MAD2B, REV7 (Homo sapiens), REV3L, POLZ, REV3 (Clostridium acetobutylicum), REV1, REV1L (Homo sapiens) Activity: DNA-directed DNA polymerase, with EC number 2.7.7.7 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed In addition to DNA repair pathways, cells utilize translesion DNA synthesis (TLS) to bypass DNA lesions during replication. During TLS, Y-family DNA polymerase (Poleta, Polkappa, Poli and Rev1) inserts specific nucleotide opposite preferred DNA lesions, and then Polzeta 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)-Polkappa(RIR). These two structures demonstrate that Rev1(CTD) contains separate binding sites for Polkappa 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 Polkappa 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. Structural insights into the assembly of human translesion polymerase complexes.,Xie W, Yang X, Xu M, Jiang T Protein Cell. 2012 Nov;3(11):864-74. doi: 10.1007/s13238-012-2102-x. Epub 2012, Nov 10. PMID:23143872 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also DNA polymerase

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