Crystal structure of PAV1-137: a protein from the virus PAV1 that infects Pyrococcus abyssi.

N. Leulliot 1, 2 S. Quevillon-Cheruel 1 M. Graille 1, 3 C. Geslin 4 D. Flament 4 M. Le Romancer 4 H. Van Tilbeurgh 1, *
* Auteur correspondant
1 IBBMC - Institut de biochimie et biophysique moléculaire et cellulaire
2 LCRB - UMR 8015 - Laboratoire de cristallographie et RMN biologiques
3 BIOC - Laboratoire de Biochimie de l'Ecole polytechnique
4 LM2E - Laboratoire de microbiologie des environnements extrêmophiles
Abstract : 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 Å. The protein forms dimers both in solution and in the crystal. The fold of PAV1-137 is a four- α -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.
Keywords : ARCHAEAL VIRUS PREDICTION PARTICLES GENOMES DOMAIN HIS1
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Article dans une revue
Archaea, Hindawi Publishing Corporation, 2013, 2013, pp.568053. 〈10.1155/2013/568053〉
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N. Leulliot, S. Quevillon-Cheruel, M. Graille, C. Geslin, D. Flament, et al.. Crystal structure of PAV1-137: a protein from the virus PAV1 that infects Pyrococcus abyssi.. Archaea, Hindawi Publishing Corporation, 2013, 2013, pp.568053. 〈10.1155/2013/568053〉. 〈hal-00834332〉

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