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3U6X

Phage TP901-1 baseplate tripod

Summary for 3U6X
Entry DOI10.2210/pdb3u6x/pdb
Related2F0C 3EJC 3UH8 4DIV 4DIW
DescriptorBPP, ORF48, BROMIDE ION, ... (4 entities in total)
Functional Keywordshelix/beta, receptor binding complex, phage tail baseplate, viral protein
Biological sourceLactococcus phage TP901-1
More
Total number of polymer chains24
Total formula weight382560.36
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: 2011-10-13, release date: 2012-07-04, Last modification date: 2023-09-13)
Primary citationVeesler, 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: 22611190
DOI: 10.1073/pnas.1200966109
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.6 Å)
Structure validation

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