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| Intimin |
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94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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| Intimin |
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94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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| Intimin |
|
94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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| Intimin |
|
94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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| Intimin |
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94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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| Intimin |
|
94-kDa outer-membrane protein encoded in the LEE. N-terminus of intimin anchors the protein in the EHEC outer membrane and exhibits little sequence variation. C-terminal end of intimin extends from the EHEC surface, binds to Tir, and exhibits extreme sequence variation that may be involved in tissue tropism. To date, sequence variations of the C-terminus have been proposed to define at least nine intmin subtypes represented by the Greek letters α through . The structure of the C-terminal end of intimin, alone (PDB code: 1F00)and in complex with Tir (PDB code: 1F02), has been determined. This region of intimin is composed of three tandem Ig-like domains followed by a C-type lectin-like domain that contains the Tir binding site. ... |
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Pet
(Plasmid-encoded enterotoxin) |
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Belongs to SPATEs subfamily. Encoded on the large virulence plasmid in close proximity to the gene encoding the AAF. ... |
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Pet
(Plasmid-encoded enterotoxin) |
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Belongs to SPATEs subfamily. Encoded on the large virulence plasmid in close proximity to the gene encoding the AAF. ... |
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Pet
(Plasmid-encoded enterotoxin) |
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Belongs to SPATEs subfamily. Encoded on the large virulence plasmid in close proximity to the gene encoding the AAF. ... |
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Pet
(Plasmid-encoded enterotoxin) |
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Belongs to SPATEs subfamily. Encoded on the large virulence plasmid in close proximity to the gene encoding the AAF. ... |
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