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1r52

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{{STRUCTURE_1r52| PDB=1r52 | SCENE= }}
{{STRUCTURE_1r52| PDB=1r52 | SCENE= }}
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'''Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae'''
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===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.
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(as it appears on PubMed at http://www.pubmed.gov), where 14573601 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14573601}}
==About this Structure==
==About this Structure==
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[[Category: Tilbeurgh, H van.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:05:11 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 19:36:43 2008''

Revision as of 16:36, 27 July 2008

Template:STRUCTURE 1r52

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

Template:ABSTRACT PUBMED 14573601

About this Structure

1R52 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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