1WOC

Crystal structure of PriB

Summary for 1WOC

• Entry DOI: 10.2210/pdb1woc/pdb
• Descriptor: Primosomal replication protein n (2 entities in total)
• Functional Keywords: oligonucleotide binding fold, dna binding protein
• Biological source: Escherichia coli
• Total number of polymer chains: 4
• Total formula weight: 45687.16

Authors

Shioi, S.,Ose, T.,Maenaka, K.,Abe, Y.,Kohda, D.,Katayama, T.,Ueda, T. (deposition date: 2004-08-13, release date: 2005-01-25, Last modification date: 2024-11-20)

Primary citation

Shioi, S.,Ose, T.,Maenaka, K.,Shiroishi, M.,Abe, Y.,Kohda, D.,Katayama, T.,Ueda, T.
Crystal structure of a biologically functional form of PriB from Escherichia coli reveals a potential single-stranded DNA-binding site
Biochem.Biophys.Res.Commun., 326:766-776, 2005

PubMed Abstract: PriB is not only an essential protein necessary for the replication restart on the collapsed and disintegrated replication fork, but also an important protein for assembling of primosome onto PhiX174 genomic DNA during replication initiation. Here we report a 2.0-A-resolution X-ray structure of a biologically functional form of PriB from Escherichia coli. The crystal structure revealed that despite a low level of primary sequence identity, the PriB monomer, as well as the dimeric form, are structurally identical to the N-terminal DNA-binding domain of the single-stranded DNA-binding protein (SSB) from Escherichia coli, which possesses an oligonucleotides-binding-fold. The oligonucleotide-PriB complex model based on the oligonucleotides-SSB complex structure suggested that PriB had a DNA-binding pocket conserved in SSB from Escherichia coli and might bind to single-stranded DNA in the manner of SSB. Furthermore, surface plasmon resonance analysis and fluorescence measurements demonstrated that PriB binds single-stranded DNA with high affinity, by involving tryptophan residue. The significance of these results with respect to the functional role of PriB in the assembly of primosome is discussed.

PubMed: 15607735
DOI: 10.1016/j.bbrc.2004.11.104

Experimental method

X-RAY DIFFRACTION (2 Å)