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Literature summary extracted from

  • Biswas, T.; Pawale, V.S.; Choudhury, D.; Roy, R.P.
    Sorting of LPXTG peptides by archetypal sortase A: role of invariant substrate residues in modulating the enzyme dynamics and conformational signature of a productive substrate (2014), Biochemistry, 53, 2515-2524.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.4.22.70 drug development the enzyme is a bona fide drug target Staphylococcus aureus
3.4.22.70 synthesis SrtA works as a versatile tool in protein engineering Staphylococcus aureus

Protein Variants

EC Number Protein Variants Comment Organism
3.4.22.70 additional information the enzyme works as a versatile tool in protein engineering. Surface proteins destined for cell wall anchoring contain a LPXTG sequence located in their C-terminus which serves as a substrate recognition motif for the enzyme Staphylococcus aureus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.4.22.70 additional information Staphylococcus aureus Surface proteins destined for cell wall anchoring contain a LPXTG sequence located in their C-terminus which serves as a substrate recognition motif for SrtA ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
3.4.22.70 Staphylococcus aureus
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.4.22.70 additional information Surface proteins destined for cell wall anchoring contain a LPXTG sequence located in their C-terminus which serves as a substrate recognition motif for SrtA Staphylococcus aureus ?
-
?

Synonyms

EC Number Synonyms Comment Organism
3.4.22.70 SrtA
-
Staphylococcus aureus

General Information

EC Number General Information Comment Organism
3.4.22.70 additional information substrate-induced conformational dynamics in the enzyme, roles of invariant Leu and Pro residues of the substrate in modulating the enzyme dynamics, analysis of the selection process of a catalytically competent substrate, molecular dynamics simulations with noncanonical substrates, overview. The linked conformation due to Pro in LPXTG is obligatory for productive binding but does not per se control the enzyme dynamics. The Leu residue of the substrate appears to play the crucial role of an anchor to the beta6-beta7 loop directing the conformational transition of the enzyme from an open to a closed state subsequent to which the Pro residue facilitates the consummation of binding through predominant engagement of the loop and catalytic motif residues in hydrophobic interactions, molecular dynamics simulations, overview Staphylococcus aureus