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  Structure and function of threonine synthase from yeast

Garrido-Franco, M., Ehlert, S., Messerschmidt, A., Marinkovic, S., Huber, R., Laber, B., et al. (2002). Structure and function of threonine synthase from yeast. Journal of Biological Chemistry, 277(14), 12396-12405.

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Genre: Journal Article
Alternative Title : J. Biol. Chem.

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 Creators:
Garrido-Franco, M.1, Author              
Ehlert, S.1, Author              
Messerschmidt, A.1, 2, Author              
Marinkovic, S.1, Author              
Huber, R.1, Author              
Laber, B., Author
Bourenkov, G. P.3, Author              
Clausen, T.1, Author              
Affiliations:
1Huber, Robert / Structure Research, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565155              
2Mann, Matthias / Proteomics and Signal Transduction, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565159              
3External Organizations, ou_persistent22              

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 Abstract: Threonine synthase catalyzes the final step of threonine biosynthesis, the pyridoxal 5'-phosphate (PLP)-dependent conversion of O-phosphohomoserine into threonine and inorganic phosphate. Threonine is an essential nutrient for mammals, and its biosynthetic machinery is restricted to bacteria, plants, and fungi; therefore, threonine synthase represents an interesting pharmaceutical target. The crystal structure of threonine synthase from Saccharomyces cerevisiae has been solved at 2.7 Angstrom resolution using multiwavelength anomalous diffraction. The structure reveals a monomer as active unit, which is subdivided into three distinct domains: a small N-terminal domain, a PLP-binding domain that covalently anchors the cofactor and a so-called large domain, which contains the main of the protein body. All three domains show the typical open alpha/beta architecture. The cofactor is bound at the interface of all three domains, buried deeply within a wide canyon that penetrates the whole molecule. Based on structural alignments with related enzymes, an enzyme-substrate complex was modeled into the active site of yeast threonine synthase, which revealed essentials for substrate binding and catalysis. Furthermore, the comparison with related enzymes of the beta-family of PLP-dependent enzymes indicated structural determinants of the oligomeric state and thus rationalized for the first time how a PLP enzyme acts in monomeric form.

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Language(s): eng - English
 Dates: 2002-04-05
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Type: Peer
 Identifiers: eDoc: 39205
ISI: 000174846400105
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Title: Journal of Biological Chemistry
  Alternative Title : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 277 (14) Sequence Number: - Start / End Page: 12396 - 12405 Identifier: ISSN: 0021-9258