ArticleThe Journal of biological chemistry2006
Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex.
Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Distal Mutations in the β-Clamp of DNA Polymerase III* Disrupt DNA Orientation and Affect Exonuclease Activity.Journal of the American Chemical Society · 2023Article
- In vivo evolution of an emerging zoonotic bacterial pathogen in an immunocompromised human host.Nature communications · 2021Article
- A structural view of bacterial DNA replication.Protein science : a publication of the Protein Society · 2019Review
- Optimizing model representation for integrative structure determination of macromolecular assemblies.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Computational Simulations of DNA Polymerases: Detailed Insights on Structure/Function/Mechanism from Native Proteins to Cancer Variants.Chemical research in toxicology · 2017Article
- Variants of sequence family B Thermococcus kodakaraensis DNA polymerase with increased mismatch extension selectivity.PloS one · 2017Article
- Thermodynamics of Macromolecular Association in Heterogeneous Crowding Environments: Theoretical and Simulation Studies with a Simplified Model.The journal of physical chemistry. B · 2016Article
- Article
- Proofreading exonuclease on a tether: the complex between the E. coli DNA polymerase III subunits α, epsilon, θ and β reveals a highly flexible arrangement of the proofreading domain.Nucleic acids research · 2013Article
- Stabilization of the Escherichia coli DNA polymerase III ε subunit by the θ subunit favors in vivo assembly of the Pol III catalytic core.Archives of biochemistry and biophysics · 2012Article
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- Defects in DNA degradation revealed in crystal structures of TREX1 exonuclease mutations linked to autoimmune disease.DNA repair · 2012Article
- Characterization and crystal structure of the type IIG restriction endonuclease RM.BpuSI.Nucleic acids research · 2011Article
- Protein-protein HADDocking using exclusively pseudocontact shifts.Journal of biomolecular NMR · 2011Article
- dnaX36 Mutator of Escherichia coli: effects of the {tau} subunit of the DNA polymerase III holoenzyme on chromosomal DNA replication fidelity.Journal of bacteriology · 2011Article
- Alteration of oligomeric state and domain architecture is essential for functional transformation between transferase and hydrolase with the same scaffold.Protein science : a publication of the Protein Society · 2009Article
- Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences.Biophysical journal · 2009Article
- Reaction mechanism of the epsilon subunit of E. coli DNA polymerase III: insights into active site metal coordination and catalytically significant residues.Journal of the American Chemical Society · 2009Article
- The proofreading exonuclease subunit epsilon of Escherichia coli DNA polymerase III is tethered to the polymerase subunit alpha via a flexible linker.Nucleic acids research · 2008Article
- Numbat: an interactive software tool for fitting Deltachi-tensors to molecular coordinates using pseudocontact shifts.Journal of biomolecular NMR · 2008Article
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Authors and funding
9 authors.
Funding
Abstract
The epsilon subunit of Escherichia coli DNA polymerase III possesses 3'-exonucleolytic proofreading activity. Within the Pol III core, epsilon is tightly bound between the alpha subunit (DNA polymerase) and subunit. Here, we present the crystal structure of epsilon in complex with HOT, the bacteriophage P1-encoded homolog of , at 2.1 A resolution. The epsilon-HOT interface is defined by two areas of contact: an interaction of the previously unstructured N terminus of HOT with an edge of the epsilon central beta-sheet as well as interactions between HOT and the catalytically important helix alpha1-loop-helix alpha2 motif of epsilon. This structure provides insight into how HOT and, by implication, may stabilize the epsilon subunit, thus promoting efficient proofreading during chromosomal replication.
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