1V1Q

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

1V1Q の概要

• エントリーDOI: 10.2210/pdb1v1q/pdb
• 分子名称: PRIMOSOMAL REPLICATION PROTEIN N, CYSTEINE (3 entities in total)
• 機能のキーワード: primosome, dna replication, dna binding
• 由来する生物種: ESCHERICHIA COLI
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 29947.45

構造登録者

Liu, J.-H.,Chang, T.-W.,Huang, C.-Y.,Chang, M.-C.,Chen, S.-U.,Wu, H.-N.,Hsiao, C.-D. (登録日: 2004-04-22, 公開日: 2004-10-25, 最終更新日: 2024-11-20)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.1 Å)