1V1Q

Crystal structure of PriB- a primosomal DNA replication protein of Escherichia coli

Summary for 1V1Q

• Entry DOI: 10.2210/pdb1v1q/pdb
• Descriptor: PRIMOSOMAL REPLICATION PROTEIN N, CYSTEINE (3 entities in total)
• Functional Keywords: primosome, dna replication, dna binding
• Biological source: ESCHERICHIA COLI
• Total number of polymer chains: 2
• Total formula weight: 29947.45

Authors

Liu, J.-H.,Chang, T.-W.,Huang, C.-Y.,Chang, M.-C.,Chen, S.-U.,Wu, H.-N.,Hsiao, C.-D. (deposition date: 2004-04-22, release date: 2004-10-25, Last modification date: 2024-11-20)

Primary citation

Liu, J.-H.,Chang, T.-W.,Huang, C.-Y.,Chen, S.-U.,Wu, H.-N.,Chang, M.-C.,Hsiao, C.-D.
Crystal Structure of Prib- a Primosomal DNA Replication Protein of Escherichia Coli
J.Biol.Chem., 279:50465-, 2004

PubMed Abstract: PriB is one of the Escherichia coli varphiX-type primosome proteins that are required for assembly of the primosome, a mobile multi-enzyme complex responsible for the initiation of DNA replication. Here we report the crystal structure of the E. coli PriB at 2.1 A resolution by multi-wavelength anomalous diffraction using a mercury derivative. The polypeptide chain of PriB is structurally similar to that of single-stranded DNA-binding protein (SSB). However, the biological unit of PriB is a dimer, not a homotetramer like SSB. Electrophoretic mobility shift assays demonstrated that PriB binds single-stranded DNA and single-stranded RNA with comparable affinity. We also show that PriB binds single-stranded DNA with certain base preferences. Based on the PriB structural information and biochemical studies, we propose that the potential tetramer formation surface and several other regions of PriB may participate in protein-protein interaction during DNA replication. These findings may illuminate the role of PriB in varphiX-type primosome assembly.

PubMed: 15383524
DOI: 10.1074/JBC.M406773200

Experimental method

X-RAY DIFFRACTION (2.1 Å)