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Literature summary extracted from

  • Kappel, K.; Wereszczynski, J.; Clubb, R.T.; McCammon, J.A.
    The binding mechanism, multiple binding modes, and allosteric regulation of Staphylococcus aureus sortase A probed by molecular dynamics simulations (2012), Protein Sci., 21, 1858-1871.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
3.4.22.70 wild-type enzyme SrtA apo and mutant enzyme C184A bound to LPETG peptide sequence, crystal structure analysis Staphylococcus aureus

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.70 Staphylococcus aureus Q95446
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-

Synonyms

EC Number Synonyms Comment Organism
3.4.22.70 sortase A
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 Staphylococcus aureus
3.4.22.70 SrtA
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 Staphylococcus aureus

General Information

EC Number General Information Comment Organism
3.4.22.70 additional information binding mechanism is a conformational selection followed by induced fit, and allosteric regulation of the enzyme, molecular dynamics simulations of the enzyme in apo state and when bound to an LPATG sorting signal, which adopts multiple metastable states, overview. The first and the second substrate binding sites are proposed to be located on opposing faces of the protein. The active sites of all sortases contain a conserved catalytic triad that consists of residues H120, C184, and R197. NMR SrtA structure covalently bound to a modified sorting signal, binding conformations, overview Staphylococcus aureus