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| ShdA |
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ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| ShdA |
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ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| ShdA |
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ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| ShdA |
|
ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| ShdA |
|
ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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| ShdA |
|
ShdA passenger domain consists of ~1,500 amino acid residues that can be divided into two regions based on features of the primary amino acid sequence: an N-terminal nonrepeat region followed by a repeat region composed of two types of imperfect direct amino acid repeats, called type A and type B. The repeat region bound fibronectin with an affinity similar to that for the complete ShdA passenger domain. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
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Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
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Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
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Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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IcsA (VirG)
(Ics for intercellular spread) |
|
Three distinctive domains: the N-terminal signal sequence (1-52), the 706 α-domain (53-758), the 344 C-terminal β-core. β-core embedded in the outer membrane, the C-terminal ~220 aa of IcsAα (509-729) are essential for the unipolar distribution of IcsA, the residues (103-433) are the binding site for N-WASP. residues (53-506) is the region of vinculin interaction and is essential for F-actin assembly. ... |
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