ArticleJournal of bacteriology2006
Structure of the theta subunit of Escherichia coli DNA polymerase III in complex with the epsilon subunit.
Article in Journal of bacteriology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- A structural view of bacterial DNA replication.Protein science : a publication of the Protein Society · 2019Review
- The Macromolecular Machines that Duplicate the Escherichia coli Chromosome as Targets for Drug Discovery.Antibiotics (Basel, Switzerland) · 2018Review
- Self-correcting mismatches during high-fidelity DNA replication.Nature structural & molecular biology · 2017Article
- An encodable lanthanide binding tag with reduced size and flexibility for measuring residual dipolar couplings and pseudocontact shifts in large proteins.Journal of biomolecular NMR · 2016Article
- DNA Polymerase α Subunit Residues and Interactions Required for Efficient Initiation Complex Formation Identified by a Genetic Selection.The Journal of biological chemistry · 2015Article
- Mutations that Separate the Functions of the Proofreading Subunit of the Escherichia coli Replicase.G3 (Bethesda, Md.) · 2015Article
- Evidence for moonlighting functions of the θ subunit of Escherichia coli DNA polymerase III.Journal of bacteriology · 2014Article
- 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
- Architecture and conservation of the bacterial DNA replication machinery, an underexploited drug target.Current drug targets · 2012Review
- NMR as a unique tool in assessment and complex determination of weak protein-protein interactions.Topics in current chemistry · 2012Review
- Protein-protein HADDocking using exclusively pseudocontact shifts.Journal of biomolecular NMR · 2011Article
- Essential biological processes of an emerging pathogen: DNA replication, transcription, and cell division in Acinetobacter spp.Microbiology and molecular biology reviews : MMBR · 2010Review
- Effect of macromolecular crowding on protein binding stability: modest stabilization and significant biological consequences.Biophysical journal · 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
- Assignment of paramagnetic (15)N-HSQC spectra by heteronuclear exchange spectroscopy.Journal of biomolecular NMR · 2007Article
- Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex.The Journal of biological chemistry · 2006Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The catalytic core of Escherichia coli DNA polymerase III contains three tightly associated subunits, the alpha, epsilon, and theta subunits. The theta subunit is the smallest and least understood subunit. The three-dimensional structure of theta in a complex with the unlabeled N-terminal domain of the epsilon subunit, epsilon186, was determined by multidimensional nuclear magnetic resonance spectroscopy. The structure was refined using pseudocontact shifts that resulted from inserting a lanthanide ion (Dy3+, Er3+, or Ho3+) at the active site of epsilon186. The structure determination revealed a three-helix bundle fold that is similar to the solution structures of theta in a methanol-water buffer and of the bacteriophage P1 homolog, HOT, in aqueous buffer. Conserved nuclear Overhauser enhancement (NOE) patterns obtained for free and complexed theta show that most of the structure changes little upon complex formation. Discrepancies with respect to a previously published structure of free theta (Keniry et al., Protein Sci. 9:721-733, 2000) were attributed to errors in the latter structure. The present structure satisfies the pseudocontact shifts better than either the structure of theta in methanol-water buffer or the structure of HOT. satisfies these shifts. The epitope of epsilon186 on theta was mapped by NOE difference spectroscopy and was found to involve helix 1 and the C-terminal part of helix 3. The pseudocontact shifts indicated that the helices of theta are located about 15 A or farther from the lanthanide ion in the active site of epsilon186, in agreement with the extensive biochemical data for the theta-epsilon system.
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