9p9a

DnaB complex binding with ssDNA and dTDP-AlFx

Structural highlights

9p9a is a 7 chain structure with sequence from Geobacillus stearothermophilus and Synthetic construct. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Electron Microscopy, Resolution 3.5Å
Ligands:	ALF, MG, TYD
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DNAB_GEOSE The main replicative DNA helicase, it participates in initiation and elongation during chromosome replication. Travels ahead of the DNA replisome, separating double-stranded (ds)DNA into templates for DNA synthesis. Binding of single-stranded (ss)DNA to the hexamer suggests a 2-nucleotide step size for the helicase and a hand-over-hand mechanism of DNA unwinding (Probable) (PubMed:23022319). Has ssDNA-stimulated ATPase activity (PubMed:10625492). DnaG primase stimulates the helicase activity (the helicase direction was not determine but is probably 5'-3') (PubMed:10625492, PubMed:12235389, PubMed:23022319). Loaded onto DNA by helicase loader DnaI (shown with DnaI of B.subtilis); ATP-binding enhances loading and subsequent ATP hydrolysis dissociates the complex, leaving helicase on the DNA (PubMed:17003052). Binds ssDNA and less well dsDNA, in the presence of ADPNP (probably 5'-adenylyl beta, gamma-imidodiphosphate, but not ATP) binding to both DNAs is improved (PubMed:12235389, PubMed:17003052).^[1] ^[2] ^[3] ^[4]

References

↑ Bird LE, Pan H, Soultanas P, Wigley DB. Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry. 2000 Jan 11;39(1):171-82. PMID:10625492 doi:10.1021/bi9918801
↑ Soultanas P, Wigley DB. Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus. Nucleic Acids Res. 2002 Sep 15;30(18):4051-60. PMID:12235389 doi:10.1093/nar/gkf527
↑ Ioannou C, Schaeffer PM, Dixon NE, Soultanas P. Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis. Nucleic Acids Res. 2006;34(18):5247-58. PMID:17003052 doi:10.1093/nar/gkl690
↑ Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation. Cell. 2012 Oct 12;151(2):267-77. doi: 10.1016/j.cell.2012.09.014. Epub 2012 Sep, 27. PMID:23022319 doi:https://dx.doi.org/10.1016/j.cell.2012.09.014

Proteopedia Page Contributors and Editors (what is this?)

OCA

[1] Bird LE, Pan H, Soultanas P, Wigley DB. Mapping protein-protein interactions within a stable complex of DNA primase and DnaB helicase from Bacillus stearothermophilus. Biochemistry. 2000 Jan 11;39(1):171-82. PMID:10625492 doi:10.1021/bi9918801

[2] Soultanas P, Wigley DB. Site-directed mutagenesis reveals roles for conserved amino acid residues in the hexameric DNA helicase DnaB from Bacillus stearothermophilus. Nucleic Acids Res. 2002 Sep 15;30(18):4051-60. PMID:12235389 doi:10.1093/nar/gkf527

[3] Ioannou C, Schaeffer PM, Dixon NE, Soultanas P. Helicase binding to DnaI exposes a cryptic DNA-binding site during helicase loading in Bacillus subtilis. Nucleic Acids Res. 2006;34(18):5247-58. PMID:17003052 doi:10.1093/nar/gkl690

[4] Itsathitphaisarn O, Wing RA, Eliason WK, Wang J, Steitz TA. The Hexameric Helicase DnaB Adopts a Nonplanar Conformation during Translocation. Cell. 2012 Oct 12;151(2):267-77. doi: 10.1016/j.cell.2012.09.014. Epub 2012 Sep, 27. PMID:23022319 doi:https://dx.doi.org/10.1016/j.cell.2012.09.014

[1]

[2]

[3]

[4]

9p9a

DnaB complex binding with ssDNA and dTDP-AlFx

Structural highlights

Function

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Navigation menu

Page actions

Page actions

Personal tools

Navigation

Search

Tools