3UH8
N-terminal domain of phage TP901-1 ORF48
Summary for 3UH8
| Entry DOI | 10.2210/pdb3uh8/pdb |
| Related | 2F0C 3EJC 3U6X |
| Descriptor | ORF48 (2 entities in total) |
| Functional Keywords | all beta protein, immunoglobulin fold, structural protein, tp901-1 orf46 and orf49, phage baseplate, viral protein |
| Biological source | Lactococcus phage TP901-1 |
| Total number of polymer chains | 1 |
| Total formula weight | 14443.05 |
| Authors | Veesler, D.,Spinelli, S.,Mahony, J.,Lichiere, J.,Blangy, S.,Bricogne, G.,Legrand, P.,Ortiz-Lombardia, M.,Campanacci, V.I.,van Sinderen, D.,Cambillau, C. (deposition date: 2011-11-03, release date: 2012-05-30, Last modification date: 2024-02-28) |
| Primary citation | Veesler, D.,Spinelli, S.,Mahony, J.,Lichiere, J.,Blangy, S.,Bricogne, G.,Legrand, P.,Ortiz-Lombardia, M.,Campanacci, V.,van Sinderen, D.,Cambillau, C. Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism. Proc.Natl.Acad.Sci.USA, 109:8954-8958, 2012 Cited by PubMed Abstract: Phages of the Caudovirales order possess a tail that recognizes the host and ensures genome delivery upon infection. The X-ray structure of the approximately 1.8 MDa host adsorption device (baseplate) from the lactococcal phage TP901-1 shows that the receptor-binding proteins are pointing in the direction of the host, suggesting that this organelle is in a conformation ready for host adhesion. This result is in marked contrast with the lactococcal phage p2 situation, whose baseplate is known to undergo huge conformational changes in the presence of Ca(2+) to reach its active state. In vivo infection experiments confirmed these structural observations by demonstrating that Ca(2+) ions are required for host adhesion among p2-like phages (936-species) but have no influence on TP901-1-like phages (P335-species). These data suggest that these two families rely on diverse adhesion strategies which may lead to different signaling for genome release. PubMed: 22611190DOI: 10.1073/pnas.1200966109 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
Download full validation report
