Wyszukiwarka
Dimeric structure of the N-terminal domain of PriB protein from Thermoanaerobacter tengcongensis solved ab initio
Abstrakt
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.
Autorzy (7)
-
Dorothee Liebschner
-
Krzysztof Brzezinski
Cytuj jako
Pełna treść
- Wersja publikacji
- Accepted albo Published Version
- Licencja
- Copyright (2012 International Union of Crystallography)
Słowa kluczowe
Informacje szczegółowe
- Kategoria:
- Publikacja w czasopiśmie
- Typ:
- artykuł w czasopiśmie wyróżnionym w JCR
- Opublikowano w:
-
Acta Crystallographica Section D-Structural Biology
nr D68,
strony 1680 - 1689,
ISSN: 2059-7983 - Język:
- angielski
- Rok wydania:
- 2012
- Opis bibliograficzny:
- 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 CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY. -Vol. D68, (2012), s.1680-1689
- Weryfikacja:
- Politechnika Gdańska
wyświetlono 96 razy
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