5TJT

T5 bacteriophage major capsid protein - one PB8 hexon

Summary for 5TJT

• Entry DOI: 10.2210/pdb5tjt/pdb
• EMDB information: 8419 8423
• Descriptor: Major capsid protein (1 entity in total)
• Functional Keywords: capsid, hk97 fold, hexon, viral protein
• Biological source: Escherichia phage T5
• Total number of polymer chains: 6
• Total formula weight: 197588.15

Authors

Conway, J.,Huet, A. (deposition date: 2016-10-05, release date: 2017-02-22, Last modification date: 2024-10-30)

Primary citation

Vernhes, E.,Renouard, M.,Gilquin, B.,Cuniasse, P.,Durand, D.,England, P.,Hoos, S.,Huet, A.,Conway, J.F.,Glukhov, A.,Ksenzenko, V.,Jacquet, E.,Nhiri, N.,Zinn-Justin, S.,Boulanger, P.
High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid.
Sci Rep, 7:41662-41662, 2017

PubMed Abstract: Bacteriophage capsids constitute icosahedral shells of exceptional stability that protect the viral genome. Many capsids display on their surface decoration proteins whose structure and function remain largely unknown. The decoration protein pb10 of phage T5 binds at the centre of the 120 hexamers formed by the major capsid protein. Here we determined the 3D structure of pb10 and investigated its capsid-binding properties using NMR, SAXS, cryoEM and SPR. Pb10 consists of an α-helical capsid-binding domain and an Ig-like domain exposed to the solvent. It binds to the T5 capsid with a remarkably high affinity and its binding kinetics is characterized by a very slow dissociation rate. We propose that the conformational exchange events observed in the capsid-binding domain enable rearrangements upon binding that contribute to the quasi-irreversibility of the pb10-capsid interaction. Moreover we show that pb10 binding is a highly cooperative process, which favours immediate rebinding of newly dissociated pb10 to the 120 hexamers of the capsid protein. In extreme conditions, pb10 protects the phage from releasing its genome. We conclude that pb10 may function to reinforce the capsid thus favouring phage survival in harsh environments.

PubMed: 28165000
DOI: 10.1038/srep41662

Experimental method

ELECTRON MICROSCOPY (9 Å)