1y7l
From Proteopedia
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O-Acetylserine Sulfhydrylase Complex
Overview
The biosynthesis of cysteine in bacteria and plants is carried out by a, two-step pathway, catalyzed by serine acetyltransferase (SAT) and, O-acetylserine sulfhydrylase (OASS; O-acetylserine [thiol] lyase). The, aerobic form of OASS forms a tight bienzyme complex with SAT in vivo, termed cysteine synthase. We have determined the crystal structure of OASS, in complex with a C-terminal peptide of SAT required for bienzyme complex, formation. The binding site of the peptide is at the active site of OASS, and its C-terminal carboxyl group occupies the same anion binding pocket, as the alpha-carboxylate of the O-acetylserine substrate of OASS. These, results explain the partial inhibition of OASS by SAT on complex formation, as well as the competitive dissociation of the complex by O-acetylserine.
About this Structure
1Y7L is a Protein complex structure of sequences from Haemophilus influenzae with SO4 as ligand. Active as Cysteine synthase, with EC number 2.5.1.47 Full crystallographic information is available from OCA.
Reference
The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase., Huang B, Vetting MW, Roderick SL, J Bacteriol. 2005 May;187(9):3201-5. PMID:15838047
Page seeded by OCA on Wed Nov 21 06:37:13 2007
