ホスホエールピルビン酸カルボキシラーゼの3次元構造 : そのアロステリック阻害機構

概要

論文の詳細を見る
The first crystal structure of phosphoenolpyruvate carboxylase (PEPC) has been determined by X - ray diffraction methods at 2.8 Å resolution using Escherichia coli PEPC complexed with L - aspartate, an allosteric inhibitor of all known PEPCs. The four subunits are arranged in a "dimer - of - dimers" form. The location of the catalytic site is suggested to be near the C - terminal side of the β - barrel. The binding site for L - aspartate is located about 20 Å away from the catalytic site and four residues (Lys773, Arg832, Arg587 and Asn881) are involved in effector binding. Considering the catalytically essential Arg587 is in a highly conserved glycine - rich loop, which is characteristic of PEPC, it seems that L - aspartate causes inhibition by removing this glycine - rich loop from the catalytic site.
日本生物物理学会の論文
2001-01-25