TY  - JOUR
A1  - Seul, Anait
A1  - Müller, Jürgen J.
A1  - Andres, Dorothee
A1  - Stettner, Eva
A1  - Heinemann, Udo
A1  - Seckler, Robert
T1  - Bacteriophage P22 tailspike: structure of the complete protein and function of the interdomain linker
JF  - Acta crystallographica : Section D, Biological crystallography
N2  - Attachment of phages to host cells, followed by phage DNA ejection, represents the first stage of viral infection of bacteria. Salmonella phage P22 has been extensively studied, serving as an experimental model for bacterial infection by phages. P22 engages bacteria by binding to the sugar moiety of lipopolysaccharides using the viral tailspike protein for attachment. While the structures of the N-terminal particle-binding domain and the major receptor-binding domain of the tailspike have been analyzed individually, the three-dimensional organization of the intact protein, including the highly conserved linker region between the two domains, remained unknown. A single amino-acid exchange in the linker sequence made it possible to crystallize the full-length protein. Two crystal structures of the linker region are presented: one attached to the N-terminal domain and the other present within the complete tailspike protein. Both retain their biological function, but the mutated full-length tailspike displays a retarded folding pathway. Fitting of the full-length tailspike into a published cryo-electron microscopy map of the P22 virion requires an elastic distortion of the crystal structure. The conservation of the linker suggests a role in signal transmission from the distal tip of the molecule to the phage head, eventually leading to DNA ejection.
Y1  - 2014
U6  - https://doi.org/10.1107/S1399004714002685
SN  - 1399-0047
VL  - 70
SP  - 1336
EP  - 1345
PB  - Wiley-Blackwell
CY  - Hoboken
ER  -