4GS3

Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tencongensis solved ab initio

Summary for 4GS3

• Entry DOI: 10.2210/pdb4gs3/pdb
• Descriptor: Single-stranded DNA-binding protein (2 entities in total)
• Functional Keywords: primosome, oligonucleotide/oligosaccharide binding domain, dna binding protein
• Biological source: Thermoanaerobacter tengcongensis
• Total number of polymer chains: 1
• Total formula weight: 12211.94

Authors

Liebschner, D.,Brzezinski, K.,Dauter, M.,Dauter, Z.,Nowak, M.,Kur, J.,Olszewski, M. (deposition date: 2012-08-27, release date: 2012-09-19, Last modification date: 2024-02-28)

Primary citation

Liebschner, D.,Brzezinski, K.,Dauter, M.,Dauter, Z.,Nowak, M.,Kur, J.,Olszewski, M.
Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tengcongensis solved ab initio.
Acta Crystallogr.,Sect.D, 68:1680-1689, 2012

PubMed Abstract: PriB is one of the components of the bacterial primosome, which catalyzes the reactivation of stalled replication forks at sites of DNA damage. The N-terminal domain of the PriB protein from the thermophilic bacterium Thermoanaerobacter tengcongensis (TtePriB) was expressed and its crystal structure was solved at the atomic resolution of 1.09 Å by direct methods. The protein chain, which encompasses the first 104 residues of the full 220-residue protein, adopts the characteristic oligonucleotide/oligosaccharide-binding (OB) structure consisting of a five-stranded β-barrel filled with hydrophobic residues and equipped with four loops extending from the barrel. In the crystal two protomers dimerize, forming a six-stranded antiparallel β-sheet. The structure of the N-terminal OB domain of T. tengcongensis shows significant differences compared with mesophile PriBs. While in all other known structures of PriB a dimer is formed by two identical OB domains in separate chains, TtePriB contains two consecutive OB domains in one chain. However, sequence comparison of both the N-terminal and the C-terminal domains of TtePriB suggests that they have analogous structures and that the natural protein possesses a structure similar to a dimer of two N-terminal domains.

PubMed: 23151633
DOI: 10.1107/S0907444912041637

Experimental method

X-RAY DIFFRACTION (1.09 Å)