2CSM

TYR-BOUND T-STATE OF YEAST CHORISMATE MUTASE

2CSM の概要

• エントリーDOI: 10.2210/pdb2csm/pdb
• 分子名称: CHORISMATE MUTASE, TYROSINE (3 entities in total)
• 機能のキーワード: allosteric protein, complex (isomerase-peptide), complex (isomerase-peptide) complex, complex (isomerase/peptide)
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 29970.36

構造登録者

Straeter, N.,Hakansson, K.,Lipscomb, W.N. (登録日: 1995-11-24, 公開日: 1996-12-23, 最終更新日: 2024-02-14)

主引用文献

Strater, N.,Hakansson, K.,Schnappauf, G.,Braus, G.,Lipscomb, W.N.
Crystal structure of the T state of allosteric yeast chorismate mutase and comparison with the R state.
Proc.Natl.Acad.Sci.USA, 93:3330-3334, 1996

PubMed Abstract: The crystal structure of the tyrosine-bound T state of allosteric yeast Saccharomyces cerevisiae chorismate mutase was solved by molecular replacement at a resolution of 2.8 angstroms using a monomer of the R-state structure as the search model. The allosteric inhibitor tyrosine was found to bind in the T state at the same binding site as the allosteric activator tryptophan binds in the R state, thus defining one regulatory binding site for each monomer. Activation by tryptophan is caused by the larger steric size of its side chain, thereby pushing apart the allosteric domain of one monomer and helix H8 of the catalytic domain of the other monomer. Inhibition is caused by polar contacts of tyrosine with Arg-75 and Arg-76 of one monomer and with Gly-141, Ser-142, and Thr-145 of the other monomer, thereby bringing the allosteric and catalytic domains closer together. The allosteric transition includes an 8 degree rotation of each of the two catalytic domains relative to the allosteric domains of each monomer (domain closure). Alternatively, this transition can be described as a 15 degree rotation of the catalytic domains of the dimer relative to each other.

PubMed: 8622937
DOI: 10.1073/pnas.93.8.3330

実験手法

X-RAY DIFFRACTION (2.8 Å)