Data/hora: 01/06/2024 04:48:30

Provedor de dados: 	5	
País: 	France	
Título: 	Crystal Structure of PAV1-137: A Protein from the Virus PAV1 That Infects Pyrococcus abyssi	
Autores: 	Leulliot, N.; Quevillon-cheruel, S.; Graille, M.; Geslin, Claire; Flament, Didier; Le Romancer, Marc; Van Tilbeurgh, H.	
Data: 	2013	
Ano: 	2013	
Resumo: 	Pyrococcus abyssi virus 1 (PAV1) was the first virus particle infecting a hyperthermophilic Euryarchaeota (Pyrococcus abyssi strain GE23) that has been isolated and characterized. It is lemon shaped and is decorated with a short fibered tail. PAV1 morphologically resembles the fusiform members of the family Fuselloviridae or the genus Salterprovirus. The 18 kb dsDNA genome of PAV1 contains 25 predicted genes, most of them of unknown function. To help assigning functions to these proteins, we have initiated structural studies of the PAV1 proteome. We determined the crystal structure of a putative protein of 137 residues (PAV1-137) at a resolution of 2.2 angstrom. The protein forms dimers both in solution and in the crystal. The fold of PAV1-137 is a four-alpha-helical bundle analogous to those found in some eukaryotic adhesion proteins such as focal adhesion kinase, suggesting that PAV1-137 is involved in protein-protein interactions.	
Tipo: 	Text	
Idioma: 	Inglês	
Identificador: 	http://archimer.ifremer.fr/doc/00134/24562/22595.pdf

DOI:10.1155/2013/568053	
Editor: 	Hindawi Publishing Corporation	
Relação: 	http://archimer.ifremer.fr/doc/00134/24562/	
Formato: 	application/pdf	
Fonte: 	Archaea-an International Microbiological Journal (1472-3646) (Hindawi Publishing Corporation), 2013 , N. ID 568053 , P. 1-5	
Fonte: 	2013 N. Leulliot et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.