2ido
Structure of the E. coli Pol III epsilon-Hot proofreading complex
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OverviewOverview
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.
About this StructureAbout this Structure
2IDO is a Protein complex structure of sequences from Enterobacteria phage p21 and Escherichia coli with , and as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.
ReferenceReference
Structure of the Escherichia coli DNA polymerase III epsilon-HOT proofreading complex., Kirby TW, Harvey S, DeRose EF, Chalov S, Chikova AK, Perrino FW, Schaaper RM, London RE, Pedersen LC, J Biol Chem. 2006 Dec 15;281(50):38466-71. Epub 2006 Sep 13. PMID:16973612
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