2isq | pdb_00002isq

Crystal Structure of O-Acetylserine Sulfhydrylase from Arabidopsis Thaliana in Complex with C-Terminal Peptide from Arabidopsis Serine Acetyltransferase

spinqualitylabelsall models 2isq, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2isq is a 2 chain structure with sequence from Arath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: PLP, SO4 Related: 1z7w, 1z7y Gene: OASA1 (ARATH), SAT1 (ARATH) Activity: Cysteine synthase, with EC number 2.5.1.47 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [SAT1_ARATH] May be involved in detoxification process by mediating the production of glutathione. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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 site residues (Thr-74, Ser-75, and Gln-147) lock the C10 peptide in the binding site. C10 peptide binding blocks access to OASS catalytic residues, explaining how complex formation downregulates OASS activity. Comparison with bacterial OASS suggests that structural plasticity in the active site allows binding of SAT C termini with dissimilar sequences at structurally similar OASS active sites. Calorimetric analysis of the effect of active site mutations (T74S, S75A, S75T, and Q147A) demonstrates that these residues are important for C10 peptide binding and that changes at these positions disrupt communication between active sites in the homodimeric enzyme. We also demonstrate that the C-terminal Ile of the C10 peptide is required for molecular recognition by At-OASS. These results provide new insights into the molecular mechanism underlying formation of the Cys synthase complex and provide a structural basis for the biochemical regulation of Cys biosynthesis in plants. Structural basis for interaction of O-acetylserine sulfhydrylase and serine acetyltransferase in the Arabidopsis cysteine synthase complex.,Francois JA, Kumaran S, Jez JM Plant Cell. 2006 Dec;18(12):3647-55. Epub 2006 Dec 28. PMID:17194764 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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