Journal
JOURNAL OF BACTERIOLOGY
Volume 187, Issue 9, Pages 3201-3205Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.187.9.3201-3205.2005
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Funding
- NCI NIH HHS [CA13330, P30 CA013330] Funding Source: Medline
- NIAID NIH HHS [AI33696, R01 AI042154, R01 AI033696] Funding Source: Medline
- NIDDK NIH HHS [P60 DK020541, P30 DK020541, DK20541] Funding Source: Medline
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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 a-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.
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