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.
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 |