Sandbox 300: Difference between revisions
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The structural details of protein A were solved by the nuclear magnetic resonance method. The length of the amino acid chain of protein A contains 508 residues. The amino acids cystein and tryptophan do not occur in the amino acid sequence. The molecular weight of the described protein is 55439 Dalton and it consists of only one protein chain. | The structural details of protein A were solved by the nuclear magnetic resonance method. The length of the amino acid chain of protein A contains 508 residues. The amino acids cystein and tryptophan do not occur in the amino acid sequence. The molecular weight of the described protein is 55439 Dalton and it consists of only one protein chain. | ||
The 3D structure is build up of three α-helixes and it consists of five extracellular domains, which are designated as E, D, A, B and C. Furthermore the protein contains cell-wall spanning regions, called X | The 3D structure is build up of three α-helixes and it consists of five extracellular domains, which are designated as E, D, A, B and C. Furthermore the protein contains cell-wall spanning regions, called X<sub>r</sub> and X<sub>c</sub>, and a hydrophobic membrane spanning domain, which is distal to LPXTG and consists of 18-20 residues<ref>Hartleib, J., Köhler, N., Dickinson, R. B., Chhatwal, G. S., Sixma, J. J., M, O., Foster, T. J., et al. (2000). Protein A is the von Willebrand factor binding protein on Staphylococcus aureus, 2149-2156</ref>. Protein A exists in a secreted and a cell wall anchored form. If it is bound to the cell wall of Staphylococcus aureus it is covalently linked to the peptidoglycan via its C-terminal domain. | ||