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7RFO

SeMet Tailspike protein 4 (TSP4) phage CBA120, residues 1-335, obtained in the presence of LiSO4

Summary for 7RFO
Entry DOI10.2210/pdb7rfo/pdb
DescriptorTailspike protein (1 entity in total)
Functional Keywordstailspike protein-protein interaction, tsp4 attachment to the tail baseplate, triple beta-helix, beta jellyroll, viral protein
Biological sourceEscherichia virus CBA120
Total number of polymer chains3
Total formula weight109968.69
Authors
Chao, K.,Shang, X.,Grenfield, J.,Linden, S.B.,Nelson, D.C.,Herzberg, O. (deposition date: 2021-07-14, release date: 2022-02-23, Last modification date: 2024-11-13)
Primary citationChao, K.L.,Shang, X.,Greenfield, J.,Linden, S.B.,Alreja, A.B.,Nelson, D.C.,Herzberg, O.
Structure of Escherichia coli O157:H7 bacteriophage CBA120 tailspike protein 4 baseplate anchor and tailspike assembly domains (TSP4-N).
Sci Rep, 12:2061-2061, 2022
Cited by
PubMed Abstract: Four tailspike proteins (TSP1-4) of Escherichia coli O157:H7 bacteriophage CBA120 enable infection of multiple hosts. They form a branched complex that attaches to the tail baseplate. Each TSP recognizes a different lipopolysaccharide on the membrane of a different bacterial host. The 335 N-terminal residues of TSP4 promote the assembly of the TSP complex and anchor it to the tail baseplate. The crystal structure of TSP4-N reveals a trimeric protein comprising four domains. The baseplate anchor domain (AD) contains an intertwined triple-stranded β-helix. The ensuing XD1, XD2 and XD3 β-sheet containing domains mediate the binding of TSP1-3 to TSP4. Each of the XD domains adopts the same fold as the respective XD domains of bacteriophage T4 gp10 baseplate protein, known to engage in protein-protein interactions via its XD2 and XD3 domains. The structural similarity suggests that XD2 and XD3 of TSP4 also function in protein-protein interactions. Analytical ultracentrifugation analyses of TSP4-N and of domain deletion proteins showed how TSP4-N promotes the formation of the TSP quaternary complex. TSP1 and TSP2 bind directly to TSP4 whereas TSP3 binding requires a pre-formed TSP4-N:TSP2 complex. A 3-dimensional model of the bacteriophage CBA120 TSP complex has been developed based on the structural and ultracentrifuge information.
PubMed: 35136138
DOI: 10.1038/s41598-022-06073-2
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.02 Å)
Structure validation

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