3ZO8

Wild-type chorismate mutase of Bacillus subtilis at 1.6 A resolution

3ZO8 の概要

• エントリーDOI: 10.2210/pdb3zo8/pdb
• 関連するPDBエントリー: 3ZOP 3ZP4 3ZP7
• 分子名称: CHORISMATE MUTASE AROH (2 entities in total)
• 機能のキーワード: pseudo-alpha beta-barrel, isomerase
• 由来する生物種: BACILLUS SUBTILIS
• 細胞内の位置: Cytoplasm : P19080
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 87047.49

構造登録者

Burschowsky, D.,vanEerde, A.,Okvist, M.,Kienhofer, A.,Kast, P.,Hilvert, D.,Krengel, U. (登録日: 2013-02-20, 公開日: 2014-04-16, 最終更新日: 2023-12-20)

主引用文献

Burschowsky, D.,Van Eerde, A.,Okvist, M.,Kienhofer, A.,Kast, P.,Hilvert, D.,Krengel, U.
Electrostatic Transition State Stabilization Rather Than Reactant Destabilization Provides the Chemical Basis for Efficient Chorismate Mutase Catalysis.
Proc.Natl.Acad.Sci.USA, 111:17516-, 2014

PubMed Abstract: For more than half a century, transition state theory has provided a useful framework for understanding the origins of enzyme catalysis. As proposed by Pauling, enzymes accelerate chemical reactions by binding transition states tighter than substrates, thereby lowering the activation energy compared with that of the corresponding uncatalyzed process. This paradigm has been challenged for chorismate mutase (CM), a well-characterized metabolic enzyme that catalyzes the rearrangement of chorismate to prephenate. Calculations have predicted the decisive factor in CM catalysis to be ground state destabilization rather than transition state stabilization. Using X-ray crystallography, we show, in contrast, that a sluggish variant of Bacillus subtilis CM, in which a cationic active-site arginine was replaced by a neutral citrulline, is a poor catalyst even though it effectively preorganizes chorismate for the reaction. A series of high-resolution molecular snapshots of the reaction coordinate, including the apo enzyme, and complexes with substrate, transition state analog and product, demonstrate that an active site, which is only complementary in shape to a reactive substrate conformer, is insufficient for effective catalysis. Instead, as with other enzymes, electrostatic stabilization of the CM transition state appears to be crucial for achieving high reaction rates.

PubMed: 25422475
DOI: 10.1073/PNAS.1408512111

実験手法

X-RAY DIFFRACTION (1.59 Å)