4HR1
Structure of PAV1-137, a protein from the virus PAV1 that infects Pyrococcus abyssi.
Summary for 4HR1
| Entry DOI | 10.2210/pdb4hr1/pdb |
| Descriptor | Putative uncharacterized protein (3 entities in total) |
| Functional Keywords | helical bundle, unknown function |
| Biological source | Pyrococcus abyssi virus 1 More |
| Total number of polymer chains | 2 |
| Total formula weight | 28977.79 |
| Authors | Leulliot, N.,Quevillon-Cheruel, S.,Graille, M.,Geslin, C.,Flament, D.,Romancer, M.L.,Tilbeurgh, H.V. (deposition date: 2012-10-26, release date: 2013-06-19, Last modification date: 2024-11-13) |
| Primary citation | Leulliot, N.,Quevillon-Cheruel, S.,Graille, M.,Geslin, C.,Flament, D.,Romancer, M.L.,Tilbeurgh, H.V. Crystal structure of PAV1-137: a protein from the virus PAV1 that infects Pyrococcus abyssi Archaea, 2013:568053-568053, 2013 Cited by PubMed 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. PubMed: 23533329DOI: 10.1155/2013/568053 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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