2isq

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Revision as of 16:23, 20 November 2007 by OCA (talk | contribs) (New page: left|200px<br /><applet load="2isq" size="450" color="white" frame="true" align="right" spinBox="true" caption="2isq, resolution 2.8Å" /> '''Crystal Structure of ...)
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File:2isq.jpg


2isq, resolution 2.8Å

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

OverviewOverview

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.

About this StructureAbout this Structure

2ISQ is a Protein complex structure of sequences from Arabidopsis thaliana with SO4 and PLP as ligands. Active as Cysteine synthase, with EC number 2.5.1.47 Full crystallographic information is available from OCA.

ReferenceReference

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

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