Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid.
Journal, issue, pages	Sci Rep, Vol. 7, Page 41662, Year 2017
Publish date	Feb 6, 2017
Authors	Emeline Vernhes / Madalena Renouard / Bernard Gilquin / Philippe Cuniasse / Dominique Durand / Patrick England / Sylviane Hoos / Alexis Huet / James F Conway / Anatoly Glukhov / Vladimir Ksenzenko / Eric Jacquet / Naïma Nhiri / Sophie Zinn-Justin / Pascale Boulanger /
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 ...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.
External links	Sci Rep / PubMed:28165000 / PubMed Central
Methods	EM (single particle) / NMR (solution)
Resolution	8.0 - 9.0 Å
Structure data	8419 5tjt EMDB-8419: High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid PDB-5tjt: T5 bacteriophage major capsid protein - one PB8 hexon Method: EM (single particle) / Resolution: 9.0 Å EMDB-8423: High affinity anchoring of the decoration protein pb10 onto the bacteriophage T5 capsid Method: EM (single particle) / Resolution: 8.0 Å PDB-5lxk: NMR structure of the C-terminal domain of the Bacteriophage T5 decoration protein pb10. Method: SOLUTION NMR PDB-5lxl: NMR structure of the N-terminal domain of the Bacteriophage T5 decoration protein pb10 Method: SOLUTION NMR
Source	escherichia phage t5 (virus)
Keywords	VIRAL PROTEIN / Bacteriophage T5 Decoration Protein / capsid / HK97 fold / hexon