Literature summary for 3.4.22.70 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.

Search for more literature for 3.4.22.70

Application

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

Protein Variants

Protein Variants	Comment	Organism
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

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
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

Organism	UniProt	Comment	Textmining
Staphylococcus aureus	-	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
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

Synonyms	Comment	Organism
SrtA	-	Staphylococcus aureus

General Information

General Information	Comment	Organism
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

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Release 2023.1 (January 2023)