BAIT

OASA1

ATCYS-3A, CYTACS1, DL3480C, FCAALL.34, O-ACETHYLSERINE SULFHYDRYLASE, O-ACETYLSERINE (THIOL)LYASE, O-acetylserine (thiol) lyase (OAS-TL) isoform A1, OLD3, ONSET OF LEAF DEATH 3, AT4G14880
O-acetylserine (thiol) lyase (OAS-TL) isoform A1
Arabidopsis thaliana (Columbia)
PREY

SERAT2;1

ATSERAT2;1, F14J16.18, F14J16_18, SAT1, SAT5, SERINE ACETYLTRANSFERASE, SERINE ACETYLTRANSFERASE 1, SERINE ACETYLTRANSFERASE 5, serine acetyltransferase 2;1, AT1G55920
serine acetyltransferase 1
GO Process (2)
GO Function (1)
GO Component (4)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Arabidopsis thaliana (Columbia)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex.

Francois JA, Kumaran S, Jez JM

In plants, association of O-acetylserine sulfhydrylase (OASS) and Ser acetyltransferase (SAT) into the Cys synthase complex plays a regulatory role in sulfur assimilation and Cys biosynthesis. We determined the crystal structure of Arabidopsis thaliana OASS (At-OASS) bound with a peptide corresponding to the C-terminal 10 residues of Arabidopsis SAT (C10 peptide) at 2.9-A resolution. Hydrogen bonding interactions with key active ... [more]

Plant Cell Dec. 01, 2006; 18(12);3647-55 [Pubmed: 17194764]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
OASA1 SERAT2;1
Reconstituted Complex
Reconstituted Complex

An interaction is inferred between proteins in vitro. This can include proteins in recombinant form or proteins isolated directly from cells with recombinant or purified bait. For example, GST pull-down assays where a GST-tagged protein is first isolated and then used to fish interactors from cell lysates are considered reconstituted complexes (e.g. PUBMED: 14657240, Fig. 4A or PUBMED: 14761940, Fig. 5). This can also include gel-shifts, surface plasmon resonance, isothermal titration calorimetry (ITC) and bio-layer interferometry (BLI) experiments. The bait-hit directionality may not be clear for 2 interacting proteins. In these cases the directionality is up to the discretion of the curator.

Low-BioGRID
281044

Curated By

  • BioGRID