3K8A

Neisseria gonorrhoeae PriB

3K8A の概要

• エントリーDOI: 10.2210/pdb3k8a/pdb
• 分子名称: Putative primosomal replication protein (2 entities in total)
• 機能のキーワード: beta-barrel, ob-fold, dna binding protein
• 由来する生物種: Neisseria gonorrhoeae FA 1090
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 23481.11

構造登録者

Lopper, M.E.,Dong, J.,George, N.P.,Duckett, K.L.,DeBeer, M.A. (登録日: 2009-10-14, 公開日: 2010-01-12, 最終更新日: 2023-09-06)

主引用文献

Dong, J.,George, N.P.,Duckett, K.L.,DeBeer, M.A.,Lopper, M.E.
The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways
Nucleic Acids Res., 38:499-509, 2010

PubMed Abstract: Reactivation of repaired DNA replication forks is essential for complete duplication of bacterial genomes. However, not all bacteria encode homologs of the well-studied Escherichia coli DNA replication restart primosome proteins, suggesting that there might be distinct mechanistic differences among DNA replication restart pathways in diverse bacteria. Since reactivation of repaired DNA replication forks requires coordinated DNA and protein binding by DNA replication restart primosome proteins, we determined the crystal structure of Neisseria gonorrhoeae PriB at 2.7 A resolution and investigated its ability to physically interact with DNA and PriA helicase. Comparison of the crystal structures of PriB from N. gonorrhoeae and E. coli reveals a well-conserved homodimeric structure consisting of two oligosaccharide/oligonucleotide-binding (OB) folds. In spite of their overall structural similarity, there is significant species variation in the type and distribution of surface amino acid residues. This correlates with striking differences in the affinity with which each PriB homolog binds single-stranded DNA and PriA helicase. These results provide evidence that mechanisms of DNA replication restart are not identical across diverse species and that these pathways have likely become specialized to meet the needs of individual organisms.

PubMed: 19906704
DOI: 10.1093/nar/gkp1031

実験手法

X-RAY DIFFRACTION (2.7 Å)