4gs3
Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tencongensis solved ab initioDimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tencongensis solved ab initio
Structural highlights
FunctionPublication Abstract from PubMedPriB 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 A 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 beta-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 beta-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. Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tengcongensis solved ab initio.,Liebschner D, Brzezinski K, Dauter M, Dauter Z, Nowak M, Kur J, Olszewski M Acta Crystallogr D Biol Crystallogr. 2012 Dec;68(Pt 12):1680-9. doi:, 10.1107/S0907444912041637. Epub 2012 Nov 9. PMID:23151633[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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