3.4.22.70: sortase A
This is an abbreviated version!
For detailed information about sortase A, go to the full flat file.
Word Map on EC 3.4.22.70
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3.4.22.70
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aureus
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staphylococcus
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lpxtg
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streptococcus
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peptidoglycan
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transpeptidation
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sortase-mediated
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a-mediated
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adhesins
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bioconjugation
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antivirulence
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mutans
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anti-infective
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pilins
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transpeptidases
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oligoglycine
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cross-bridges
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pentaglycine
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wall-anchored
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molecular biology
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azide-alkyne
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analysis
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biotechnology
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drug development
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synthesis
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medicine
- 3.4.22.70
- aureus
- staphylococcus
-
lpxtg
- streptococcus
- peptidoglycan
-
transpeptidation
-
sortase-mediated
-
a-mediated
- adhesins
-
bioconjugation
-
antivirulence
- mutans
-
anti-infective
- pilins
- transpeptidases
-
oligoglycine
-
cross-bridges
- pentaglycine
-
wall-anchored
- molecular biology
-
azide-alkyne
- analysis
- biotechnology
- drug development
- synthesis
- medicine
Reaction
The enzyme catalyses a cell wall sorting reaction in which a surface protein with a sorting signal containing a LPXTG motif is cleaved between the Thr and Gly residue. The resulting threonine carboxyl end of the protein is covalently attached to a pentaglycine cross-bridge of peptidoglycan. =
Synonyms
C60.001, sortase A, sortase A transpeptidase, sortase SrtA, sortase transpeptidase, SrtA, SrtA protein, SrtA sortase
ECTree
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Crystallization
Crystallization on EC 3.4.22.70 - sortase A
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crystals are grown by the hanging-drop technique with a protein concentration of 50 mg/ml in 25 mM MES buffer, pH 6.35. The crystallization conditions include 3.2 M ammonium sulfate, 0.1 M NaCl, and trace amounts of ethylene glycol. Crystal structure of native SrtA, of an active-site mutant of SrtA, and of the mutant SrtA complexed with its substrate LPETG peptide
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wild-type enzyme SrtA apo and mutant enzyme C184A bound to LPETG peptide sequence, crystal structure analysis
hanging drop method of vapor diffusion at 20°C, SrtA residues Val82-Thr249 (catalytic domain)