PDBsum entry 3k8a

DNA binding protein

PDB id: 3k8a

Contents

Protein chains

100 a.a. *

Waters ×8

* Residue conservation analysis

PDB id:

3k8a

Name:

DNA binding protein

Title:

Neisseria gonorrhoeae prib

Structure:

Putative primosomal replication protein. Chain: a, b. Engineered: yes

Source:

Neisseria gonorrhoeae fa 1090. Organism_taxid: 242231. Strain: fa1090. Gene: ngo0582, prib. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.70Å R-factor: 0.245 R-free: 0.288

Authors:

M.E.Lopper,J.Dong,N.P.George,K.L.Duckett,M.A.Debeer

Key ref:

J.Dong et al. (2010). The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways. Nucleic Acids Res, 38, 499-509. PubMed id: 19906704

Date:

14-Oct-09 Release date: 12-Jan-10

Protein chains

Q5F924  (PRIB_NEIG1) -  Primosomal replication protein N from Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090)

Seq: 100 a.a.

Struc: 100 a.a.

Nucleic Acids Res 38:499-509 (2010)

PubMed id: 19906704

The crystal structure of Neisseria gonorrhoeae PriB reveals mechanistic differences among bacterial DNA replication restart pathways.

J.Dong, N.P.George, K.L.Duckett, M.A.DeBeer, M.E.Lopper.

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.