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| - | [[Image:1r53.jpg|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1r53| PDB=1r53 | SCENE= }} | | {{STRUCTURE_1r53| PDB=1r53 | SCENE= }} |
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| - | '''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''
| + | ===Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae=== |
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| - | ==Overview==
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| - | Chorismate synthase (EC 4.2.3.5), the seventh enzyme in the shikimate pathway, catalyzes the transformation of 5-enolpyruvylshikimate 3-phosphate (EPSP) to chorismate, which is the last common precursor in the biosynthesis of numerous aromatic compounds in bacteria, fungi, and plants. The chorismate synthase reaction involves a 1,4-trans-elimination of phosphoric acid from EPSP and has an absolute requirement for reduced FMN as a cofactor. We have determined the three-dimensional x-ray structure of the yeast chorismate synthase from selenomethionine-labeled crystals at 2.2-A resolution. The structure shows a novel betaalphabetaalpha fold consisting of an alternate tight packing of two alpha-helical and two beta-sheet layers, showing no resemblance to any documented protein structure. The molecule is arranged as a tight tetramer with D2 symmetry, in accordance with its quaternary structure in solution. Electron density is missing for 23% of the amino acids, spread over sequence regions that in the three-dimensional structure converge on the surface of the protein. Many totally conserved residues are contained within these regions, and they probably form a structured but mobile domain that closes over a cleft upon substrate binding and catalysis. This hypothesis is supported by previously published spectroscopic measurements implying that the enzyme undergoes considerable structural changes upon binding of both FMN and EPSP.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_14573601}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14573601 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14573601}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Tilbeurgh, H van.]] | | [[Category: Tilbeurgh, H van.]] |
| | [[Category: Two layers alpha-beta]] | | [[Category: Two layers alpha-beta]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:05:10 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 02:36:07 2008'' |
Revision as of 23:36, 28 July 2008
Template:STRUCTURE 1r53
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae
Template:ABSTRACT PUBMED 14573601
About this Structure
1R53 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae., Quevillon-Cheruel S, Leulliot N, Meyer P, Graille M, Bremang M, Blondeau K, Sorel I, Poupon A, Janin J, van Tilbeurgh H, J Biol Chem. 2004 Jan 2;279(1):619-25. Epub 2003 Oct 21. PMID:14573601
Page seeded by OCA on Tue Jul 29 02:36:07 2008
Categories: Chorismate synthase | Saccharomyces cerevisiae | Single protein | Blondeau, K. | Bremang, M. | Graille, M. | Janin, J. | Leulliot, N. | Meyer, P. | Poupon, A. | Quevillon-Cheruel, S. | Sorel, I. | Tilbeurgh, H van. | Two layers alpha-beta
