Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.5.1.47 extracted from

  • Francois, J.A.; Kumaran, S.; Jez, J.M.
    Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex (2006), Plant Cell, 18, 3647-3655.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.5.1.47

Crystallization (Commentary)

Crystallization (Comment) Organism
to elucidate the structural basis of protein–protein interactions in the plant Cys synthase complex, the crystal structure of Arabidopsis thaliana O-acetylserine sulfhydrylase bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase (C10 peptide) is determiend at 2.9 A resolution Arabidopsis thaliana

Protein Variants

Protein Variants Comment Organism
Q147A mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase Arabidopsis thaliana
S75A mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase Arabidopsis thaliana
S75T mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase Arabidopsis thaliana
T74S mutations reduce binding affinity for the C10 peptide corresponding to the C-terminal 10 residues of Arabidopsis serine acetyltransferase Arabidopsis thaliana

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Arabidopsis thaliana
-
-
-

Synonyms

Synonyms Comment Organism
At-OASS
-
 Arabidopsis thaliana