1997
DOI: 10.1006/jmbi.1997.0922
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Phage P22 tailspike protein: crystal structure of the head-binding domain at 2.3 Å, fully refined structure of the endorhamnosidase at 1.56 Å resolution, and the molecular basis of O-antigen recognition and cleavage

Abstract: The tailspike protein of Salmonella phage P22 is a viral adhesion protein with both receptor binding and destroying activities. It recognises the O-antigenic repeating units of cell surface lipopolysaccharide of serogroup A, B and D1 as receptor, but also inactivates its receptor by endoglycosidase (endorhamnosidase) activity. In the final step of bacteriophage P22 assembly six homotrimeric tailspike molecules are non-covalently attached to the DNA injection apparatus, mediated by their N-terminal, head-bindin… Show more

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Cited by 170 publications
(206 citation statements)
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“…However, aside from their globular shape, the C-terminal extensions share no further structural similarity with the reported CIMCDs. The parallel-β-helix tailspike proteins (TSP) of the Podoviridae bacteriophages P22, Phi29, HK620, and Sf6 all contain a C-terminal trimerization domain that predominantly consists of β-strands, unlike the CIMCDs, which are mainly α-helical [19][20][21][22][23] . In the extensively studied P22 TSP, a combination of a triple β-helix, a β-prism and an antiparallel β-sheet interact in order to form a trimerization domain 21,22 .…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…However, aside from their globular shape, the C-terminal extensions share no further structural similarity with the reported CIMCDs. The parallel-β-helix tailspike proteins (TSP) of the Podoviridae bacteriophages P22, Phi29, HK620, and Sf6 all contain a C-terminal trimerization domain that predominantly consists of β-strands, unlike the CIMCDs, which are mainly α-helical [19][20][21][22][23] . In the extensively studied P22 TSP, a combination of a triple β-helix, a β-prism and an antiparallel β-sheet interact in order to form a trimerization domain 21,22 .…”
Section: Discussionmentioning
confidence: 99%
“…The parallel-β-helix tailspike proteins (TSP) of the Podoviridae bacteriophages P22, Phi29, HK620, and Sf6 all contain a C-terminal trimerization domain that predominantly consists of β-strands, unlike the CIMCDs, which are mainly α-helical [19][20][21][22][23] . In the extensively studied P22 TSP, a combination of a triple β-helix, a β-prism and an antiparallel β-sheet interact in order to form a trimerization domain 21,22 . In the recently described neck appendages of bacteriophage Phi29, a C-terminal extension, which mainly consists of two β-barrels, aids maturation of the parallel-β-helix pre-protein in an ATP-driven reaction 23 .…”
Section: Discussionmentioning
confidence: 99%
“…The structure of the P22 trimeric TSP has been described in detail in x-ray crystallographic and cryoelectron microscopy studies, Figure 1 (Pymol representation of xray coordinates) [6][7][8][9][10][11]. The P22 TSP consists of three structural elements: 1) The P22 TSP N-terminal domain (P22 TSP NTD), containing the first 108 amino acids (aa1-aa108) from each of three TSPs, exists as a domelike structure, Figure 2 [9]. The P22 TSP NTD is necessary for P22 phage particle assembly [12].…”
Section: The Structural Domains Of the P22 Tailspike Proteinmentioning
confidence: 99%
“…Its carboxy terminus is responsible for the hydrolysis of the oligosaccharide receptor at the outer cell membrane [1], allowing the phage particles to positionate for DNA injection, while the amino terminal domain connects the TSP to the phage neck [2]. The native TSP is unusually resistant to proteolysis and to temperature-and detergent-mediated denaturation, whereas the folding intermediates are extremely thermolabile [3].…”
Section: Introductionmentioning
confidence: 99%