7RFO
SeMet Tailspike protein 4 (TSP4) phage CBA120, residues 1-335, obtained in the presence of LiSO4
Summary for 7RFO
Entry DOI | 10.2210/pdb7rfo/pdb |
Descriptor | Tailspike protein (1 entity in total) |
Functional Keywords | tailspike protein-protein interaction, tsp4 attachment to the tail baseplate, triple beta-helix, beta jellyroll, viral protein |
Biological source | Escherichia virus CBA120 |
Total number of polymer chains | 3 |
Total formula weight | 109968.69 |
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 citation | Chao, 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: 35136138DOI: 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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