1R52

Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae

1R52 の概要

• エントリーDOI: 10.2210/pdb1r52/pdb
• 関連するPDBエントリー: 1R53
• 分子名称: Chorismate synthase (2 entities in total)
• 機能のキーワード: two layers alpha-beta, lyase
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 166884.58

構造登録者

Quevillon-Cheruel, S.,Leulliot, N.,Meyer, P.,Graille, M.,Bremang, M.,Blondeau, K.,Sorel, I.,Poupon, A.,Janin, J.,van Tilbeurgh, H. (登録日: 2003-10-09, 公開日: 2003-12-23, 最終更新日: 2024-03-13)

主引用文献

Quevillon-Cheruel, S.,Leulliot, N.,Meyer, P.,Graille, M.,Bremang, M.,Blondeau, K.,Sorel, I.,Poupon, A.,Janin, J.,van Tilbeurgh, H.
Crystal structure of the bifunctional chorismate synthase from Saccharomyces cerevisiae
J.Biol.Chem., 279:619-625, 2004

PubMed Abstract: 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.

PubMed: 14573601
DOI: 10.1074/jbc.M310380200

実験手法

X-RAY DIFFRACTION (2.89 Å)