2haj

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Solution structure of the helicase-binding domain of Escherichia coli primase

Overview

DnaG is the primase that lays down RNA primers on single-stranded DNA, during bacterial DNA replication. The solution structure of the, DnaB-helicase-binding C-terminal domain of Escherichia coli DnaG was, determined by NMR spectroscopy at near-neutral pH. The structure is a rare, fold that, besides occurring in DnaG C-terminal domains, has been, described only for the N-terminal domain of DnaB. The C-terminal helix, hairpin present in the DnaG C-terminal domain, however, is either less, stable or absent in DnaB, as evidenced by high mobility of the C-terminal, 35 residues in a construct comprising residues 1-171. The present, structure identifies the previous crystal structure of the E. coli DnaG, C-terminal domain as a domain-swapped dimer. It is also significantly, different from the NMR structure reported for the corresponding domain of, DnaG from the thermophile Bacillus stearothermophilus. NMR experiments, showed that the DnaG C-terminal domain does not bind to residues 1-171 of, the E. coli DnaB helicase with significant affinity.

About this Structure

2HAJ is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase., Su XC, Schaeffer PM, Loscha KV, Gan PH, Dixon NE, Otting G, FEBS J. 2006 Nov;273(21):4997-5009. Epub 2006 Sep 28. PMID:17010164

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