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-Structure paper
Title | Structure of the phage TP901-1 1.8 MDa baseplate suggests an alternative host adhesion mechanism. |
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Journal, issue, pages | Proc. Natl. Acad. Sci. USA, Vol. 109, Page 8954-8958, Year 2012 |
Publish date | Oct 13, 2011 (structure data deposition date) |
![]() | Veesler, D. / Spinelli, S. / Mahony, J. / Lichiere, J. / Blangy, S. / Bricogne, G. / Legrand, P. / Ortiz-Lombardia, M. / Campanacci, V. / van Sinderen, D. / Cambillau, C. |
![]() | ![]() ![]() |
Methods | X-ray diffraction |
Resolution | 2.3 - 3.8 Å |
Structure data | ![]() PDB-3u6x: ![]() PDB-3uh8: ![]() PDB-4v96: |
Chemicals | ![]() ChemComp-BR: ![]() ChemComp-HOH: |
Source |
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![]() | VIRAL PROTEIN / helix/beta / receptor binding complex / phage tail baseplate / all beta protein / immunoglobulin fold / structural protein / TP901-1 ORF46 and ORF49 / phage baseplate / Distal tail protein / Receptor-binding protein / host adsorption apparatus / genome injection device |