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2KHU

Solution Structure of the Ubiquitin-Binding Motif of Human Polymerase Iota

Summary for 2KHU
Entry DOI10.2210/pdb2khu/pdb
Related2KHW
NMR InformationBMRB: 16882
DescriptorImmunoglobulin G-binding protein G, DNA polymerase iota (1 entity in total)
Functional Keywordsubm, ubiquitin-binding domain, polymerase iota, translesion synthesis, tls, immunoglobulin g-binding protein, ubiquitin-binding protein, transferase-protein binding complex, transferase/protein binding
Biological sourceStreptococcus sp., Homo sapiens
Cellular locationNucleus: Q9UNA4
Total number of polymer chains1
Total formula weight12348.56
Authors
Bomar, M.G.,D'Souza, S.,Bienko, M.,Dikic, I.,Walker, G. (deposition date: 2009-04-11, release date: 2010-02-23, Last modification date: 2024-05-22)
Primary citationBomar, M.G.,D'Souza, S.,Bienko, M.,Dikic, I.,Walker, G.C.,Zhou, P.
Unconventional Ubiquitin Recognition by the Ubiquitin-Binding Motif within the Y Family DNA Polymerases iota and Rev1.
Mol.Cell, 37:408-417, 2010
Cited by
PubMed Abstract: Translesion synthesis is an essential cell survival strategy to promote replication after DNA damage. The accumulation of Y family polymerases (pol) iota and Rev1 at the stalled replication machinery is mediated by the ubiquitin-binding motifs (UBMs) of the polymerases and enhanced by PCNA monoubiquitination. We report the solution structures of the C-terminal UBM of human pol iota and its complex with ubiquitin. Distinct from other ubiquitin-binding domains, the UBM binds to the hydrophobic surface of ubiquitin centered at L8. Accordingly, mutation of L8A, but not I44A, of ubiquitin abolishes UBM binding. Human pol iota contains two functional UBMs, both contributing to replication foci formation. In contrast, only the second UBM of Saccharomyces cerevisiae Rev1 binds to ubiquitin and is essential for Rev1-dependent cell survival and mutagenesis. Point mutations disrupting the UBM-ubiquitin interaction also impair the accumulation of pol iota in replication foci and Rev1-mediated DNA damage tolerance in vivo.
PubMed: 20159559
DOI: 10.1016/j.molcel.2009.12.038
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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