2HAJ

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

Summary for 2HAJ

• Entry DOI: 10.2210/pdb2haj/pdb
• Related: 1T3W
• NMR Information: BMRB: 6284
• Descriptor: DNA primase (1 entity in total)
• Functional Keywords: dna polymerase, helicase, primase, helix, transferase
• Biological source: Escherichia coli
• Total number of polymer chains: 1
• Total formula weight: 16718.97

Authors

Su, X.C.,Loscha, K.V.,Dixon, N.E.,Otting, G. (deposition date: 2006-06-13, release date: 2006-10-17, Last modification date: 2024-05-15)

Primary citation

Su, X.C.,Schaeffer, P.M.,Loscha, K.V.,Gan, P.H.P.,Dixon, N.E.,Otting, G.
Monomeric solution structure of the helicase-binding domain of Escherichia coli DnaG primase
Febs J., 273:4997-5009, 2006

PubMed Abstract: 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.

PubMed: 17010164
DOI: 10.1111/j.1742-4658.2006.05495.x

Experimental method

SOLUTION NMR