From Proteopedia
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Function
Fibritin (Fib) is a structural protein of virus. Fib promotes the assembly of the long tail fibers (whiskers) and their attachment to the virus tail baseplate. Fib is also responsible for the retraction of the tail fibers in adverse environment[1].
Structural highlights
. Fib structure is composed of N-terminal domain which is responsible for attachment to the phage, a central 500A domain made of triple-helix coiled coil and the C-terminal domain (foldon) – residues 458-484 – which is the trimerization domain.
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3D structures of fibritin
Updated on 28-July-2020
2bsg, 3j2o – T4Fib – T4 bacteriophage – Cryo-EM
1aa0 – T4Fib residues 371-483 – T4 bacteriophage
1avy – T4Fib residues 413-486 (mutant)
2ww6, 2ww7, 4ncu, 4ncv, 4ncw – T4Fib foldon 458-484
1u0p – T4Fib foldon - NMR
1rfo, 2kbl – T4Fib foldon (mutant) - NMR
1ox3 – T4Fib N-terminal + foldon domains
2ibl – Fib N-terminal + foldon domains – unidentified phage
1v1h, 1v1i – Fib shaft domain/T4Fib foldon domain - Adenovirus
3a1m – T4Fib foldon/GP5C
6z97 – ScvFib – SARS coronavirus – Cryo EM
6crv, 6crw, 6crx, 6crz, 6cs0, 6cs1, 6cs2 – ScvFib (mutant)
References
- ↑ Tao Y, Strelkov SV, Mesyanzhinov VV, Rossmann MG. Structure of bacteriophage T4 fibritin: a segmented coiled coil and the role of the C-terminal domain. Structure. 1997 Jun 15;5(6):789-98. PMID:9261070
