1r53: Difference between revisions

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[[Image:1r53.jpg|left|200px]]
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[[Image:1r53.png|left|200px]]


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{{STRUCTURE_1r53|  PDB=1r53  |  SCENE=  }}  
{{STRUCTURE_1r53|  PDB=1r53  |  SCENE=  }}  


'''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''
===Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae===




==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.
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{{ABSTRACT_PUBMED_14573601}}


==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]]
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Revision as of 23:36, 28 July 2008

File:1r53.png

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

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