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| | {{STRUCTURE_1kl7| PDB=1kl7 | SCENE= }} | | {{STRUCTURE_1kl7| PDB=1kl7 | SCENE= }} |
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| - | '''Crystal Structure of Threonine Synthase from Yeast'''
| + | ===Crystal Structure of Threonine Synthase from Yeast=== |
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| - | ==Overview==
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| - | 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 A 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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| | + | (as it appears on PubMed at http://www.pubmed.gov), where 11756443 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_11756443}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Pyridoxal 5-phosphate]] | | [[Category: Pyridoxal 5-phosphate]] |
| | [[Category: Threonine synthesis]] | | [[Category: Threonine synthesis]] |
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| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 10:30:15 2008'' |
Revision as of 07:30, 2 July 2008
Template:STRUCTURE 1kl7
Crystal Structure of Threonine Synthase from Yeast
Template:ABSTRACT PUBMED 11756443
About this Structure
1KL7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Structure and function of threonine synthase from yeast., Garrido-Franco M, Ehlert S, Messerschmidt A, Marinkovic' S, Huber R, Laber B, Bourenkov GP, Clausen T, J Biol Chem. 2002 Apr 5;277(14):12396-405. Epub 2001 Dec 26. PMID:11756443
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