1W85

The crystal structure of pyruvate dehydrogenase E1 bound to the peripheral subunit binding domain of E2

1W85 の概要

• エントリーDOI: 10.2210/pdb1w85/pdb
• 関連するPDBエントリー: 1B5S 1EBD 1LAB 1LAC 1W3D 1W4E 1W4F 1W4G 1W4H 1W88 2PDD 2PDE
• 分子名称: PYRUVATE DEHYDROGENASE E1 COMPONENT, ALPHA SUBUNIT, PYRUVATE DEHYDROGENASE E1 COMPONENT, BETA SUBUNIT, DIHYDROLIPOYLLYSINE-RESIDUE ACETYLTRANSFERASE COMPONENT OF PYRUVATE, ... (8 entities in total)
• 機能のキーワード: pyruvate, dehydrogenase, dihydrolipoyl, acetyl transferase, multienzyme complex, oxidoreductase, transferase
• 由来する生物種: GEOBACILLUS STEAROTHERMOPHILUS; 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 319851.73

構造登録者

Frank, R.A.W.,Pratap, J.V.,Pei, X.Y.,Perham, R.N.,Luisi, B.F. (登録日: 2004-09-16, 公開日: 2004-11-02, 最終更新日: 2023-12-13)

主引用文献

Frank, R.A.,Titman, C.M.,Pratap, J.V.,Luisi, B.F.,Perham, R.N.
A molecular switch and proton wire synchronize the active sites in thiamine enzymes.
Science, 306:872-876, 2004

PubMed Abstract: Thiamine diphosphate (ThDP) is used as a cofactor in many key metabolic enzymes. We present evidence that the ThDPs in the two active sites of the E1 (EC 1.2.4.1) component of the pyruvate dehydrogenase complex communicate over a distance of 20 angstroms by reversibly shuttling a proton through an acidic tunnel in the protein. This "proton wire" permits the co-factors to serve reciprocally as general acid/base in catalysis and to switch the conformation of crucial active-site peptide loops. This synchronizes the progression of chemical events and can account for the oligomeric organization, conformational asymmetry, and "ping-pong" kinetic properties of E1 and other thiamine-dependent enzymes.

PubMed: 15514159
DOI: 10.1126/science.1101030

実験手法

X-RAY DIFFRACTION (2 Å)