5NGJ
Crystal structure of pb6, major tail tube protein of bacteriophage T5
Summary for 5NGJ
| Entry DOI | 10.2210/pdb5ngj/pdb |
| Descriptor | Tail tube protein, CHLORIDE ION (3 entities in total) |
| Functional Keywords | bacteriophage, viral protein, tube protein, virion protein |
| Biological source | Escherichia phage T5 |
| Total number of polymer chains | 2 |
| Total formula weight | 104457.23 |
| Authors | Arnaud, C.-A.,Effantin, G.,Vives, C.,Engilberge, S.,Bacia, M.,Boulanger, P.,Girard, E.,Schoehn, G.,Breyton, C. (deposition date: 2017-03-17, release date: 2018-01-03, Last modification date: 2024-05-08) |
| Primary citation | Arnaud, C.A.,Effantin, G.,Vives, C.,Engilberge, S.,Bacia, M.,Boulanger, P.,Girard, E.,Schoehn, G.,Breyton, C. Bacteriophage T5 tail tube structure suggests a trigger mechanism for Siphoviridae DNA ejection. Nat Commun, 8:1953-1953, 2017 Cited by PubMed Abstract: The vast majority of phages, bacterial viruses, possess a tail ensuring host recognition, cell wall perforation and safe viral DNA transfer from the capsid to the host cytoplasm. Long flexible tails are formed from the tail tube protein (TTP) polymerised as hexameric rings around and stacked along the tape measure protein (TMP). Here, we report the crystal structure of T5 TTP pb6 at 2.2 Å resolution. Pb6 is unusual in forming a trimeric ring, although structure analysis reveals homology with all classical TTPs and related tube proteins of bacterial puncturing devices (type VI secretion system and R-pyocin). Structures of T5 tail tubes before and after interaction with the host receptor were determined by cryo-electron microscopy at 6 Å resolution. Comparison of these two structures reveals that host-binding information is not propagated to the capsid through conformational changes in the tail tube, suggesting a role of the TMP in this information transduction process. PubMed: 29209037DOI: 10.1038/s41467-017-02049-3 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
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