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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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ActA |
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639-amino acid protein with a 610-residue mature form that is attached to the bacterial cell wall via its C-terminal. Mature ActA can be divided into three distinct domains:. (1)N-terminal domain rich in positively charged residues, amino acids 121 to 170 contain an Arp2/3 complex-binding and activation domain, amino acids 60 to 101 is the monomeric actin binding region. (2) central region of proline-rich repeats required for binding of VASP and Mena, VASP binds profilin to recuit monomeric actin to sites of actin reorganization or by bundling of actin filaments into a tail to accelerate the actin nucleation. (3) C-terminal domain with a highly hydrophobic stretch that anchors the protein to the bacterial surface. ... |
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