This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Huang, B.
Right arrow Articles by Roderick, S. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Huang, B.
Right arrow Articles by Roderick, S. L.

 Previous Article  |  Next Article 

Journal of Bacteriology, May 2005, p. 3201-3205, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.3201-3205.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

The Active Site of O-Acetylserine Sulfhydrylase Is the Anchor Point for Bienzyme Complex Formation with Serine Acetyltransferase

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

Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York

Received 9 December 2004/ Accepted 24 January 2005

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.

* Corresponding author. Mailing address: Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Ave., Bronx, NY 10461. Phone: (718) 430-2784. Fax: (718) 430-8565. E-mail: roderick{at}aecom.yu.edu.

Journal of Bacteriology, May 2005, p. 3201-3205, Vol. 187, No. 9
0021-9193/05/$08.00+0     doi:10.1128/JB.187.9.3201-3205.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Kumaran, S., Yi, H., Krishnan, H. B., Jez, J. M. (2009). Assembly of the Cysteine Synthase Complex and the Regulatory Role of Protein-Protein Interactions. J. Biol. Chem. 284: 10268-10275 [Abstract] [Full Text]  
  • Tanous, C., Soutourina, O., Raynal, B., Hullo, M.-F., Mervelet, P., Gilles, A.-M., Noirot, P., Danchin, A., England, P., Martin-Verstraete, I. (2008). The CymR Regulator in Complex with the Enzyme CysK Controls Cysteine Metabolism in Bacillus subtilis. J. Biol. Chem. 283: 35551-35560 [Abstract] [Full Text]  
  • Agren, D., Schnell, R., Oehlmann, W., Singh, M., Schneider, G. (2008). Cysteine Synthase (CysM) of Mycobacterium tuberculosis Is an O-Phosphoserine Sulfhydrylase: EVIDENCE FOR AN ALTERNATIVE CYSTEINE BIOSYNTHESIS PATHWAY IN MYCOBACTERIA. J. Biol. Chem. 283: 31567-31574 [Abstract] [Full Text]  
  • Schnell, R., Oehlmann, W., Singh, M., Schneider, G. (2007). Structural Insights into Catalysis and Inhibition of O-Acetylserine Sulfhydrylase from Mycobacterium tuberculosis: CRYSTAL STRUCTURES OF THE ENZYME {alpha}-AMINOACRYLATE INTERMEDIATE AND AN ENZYME-INHIBITOR COMPLEX. J. Biol. Chem. 282: 23473-23481 [Abstract] [Full Text]  
  • Francois, J. A., Kumaran, S., Jez, J. M. (2006). Structural Basis for Interaction of O-Acetylserine Sulfhydrylase and Serine Acetyltransferase in the Arabidopsis Cysteine Synthase Complex. Plant Cell 18: 3647-3655 [Abstract] [Full Text]  
  • Liu, F., Yoo, B.-C., Lee, J.-Y., Pan, W., Harmon, A. C. (2006). Calcium-regulated Phosphorylation of Soybean Serine Acetyltransferase in Response to Oxidative Stress. J. Biol. Chem. 281: 27405-27415 [Abstract] [Full Text]  
  • Bonner, E. R., Cahoon, R. E., Knapke, S. M., Jez, J. M. (2005). Molecular Basis of Cysteine Biosynthesis in Plants: STRUCTURAL AND FUNCTIONAL ANALYSIS OF O-ACETYLSERINE SULFHYDRYLASE FROM ARABIDOPSIS THALIANA. J. Biol. Chem. 280: 38803-38813 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»