The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase

Bin Huang, Matthew W. Vetting, Steven L. Roderick

Research output: Contribution to journalArticle

62 Citations (Scopus)

Abstract

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 α-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.

Original languageEnglish (US)
Pages (from-to)3201-3205
Number of pages5
JournalJournal of Bacteriology
Volume187
Issue number9
DOIs
StatePublished - May 2005

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Serine O-Acetyltransferase
Cysteine Synthase
Catalytic Domain
Peptides
Anions
Cysteine
Binding Sites
Bacteria

ASJC Scopus subject areas

  • Applied Microbiology and Biotechnology
  • Immunology

Cite this

The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. / Huang, Bin; Vetting, Matthew W.; Roderick, Steven L.

In: Journal of Bacteriology, Vol. 187, No. 9, 05.2005, p. 3201-3205.

Research output: Contribution to journalArticle

Huang, Bin ; Vetting, Matthew W. ; Roderick, Steven L. / The active site of O-acetylserine sulfhydrylase is the anchor point for bienzyme complex formation with serine acetyltransferase. In: Journal of Bacteriology. 2005 ; Vol. 187, No. 9. pp. 3201-3205.
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