1C96

S642A:CITRATE COMPLEX OF ACONITASE

1C96 の概要

• エントリーDOI: 10.2210/pdb1c96/pdb
• 関連するPDBエントリー: 1C97
• 分子名称: MITOCHONDRIAL ACONITASE, CITRATE ANION, IRON/SULFUR CLUSTER, ... (5 entities in total)
• 機能のキーワード: lyase, tricarboxylic acid cycle, iron-sulfur, mitochondrion, transit peptide, 4fe-4s
• 由来する生物種: Bos taurus (cattle)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 83174.68

構造登録者

Lloyd, S.J.,Lauble, H.,Prasad, G.S.,Stout, C.D. (登録日: 1999-07-31, 公開日: 1999-08-12, 最終更新日: 2024-02-07)

主引用文献

Lloyd, S.J.,Lauble, H.,Prasad, G.S.,Stout, C.D.
The mechanism of aconitase: 1.8 A resolution crystal structure of the S642a:citrate complex.
Protein Sci., 8:2655-2662, 1999

PubMed Abstract: The crystal structure of the S642A mutant of mitochondrial aconitase (mAc) with citrate bound has been determined at 1.8 A resolution and 100 K to capture this binding mode of substrates to the native enzyme. The 2.0 A resolution, 100 K crystal structure of the S642A mutant with isocitrate binding provides a control, showing that the Ser --> Ala replacement does not alter the binding of substrates in the active site. The aconitase mechanism requires that the intermediate product, cis-aconitate, flip over by 180 degrees about the C alpha-C beta double bond. Only one of these two alternative modes of binding, that of the isocitrate mode, has been previously visualized. Now, however, the structure revealing the citrate mode of binding provides direct support for the proposed enzyme mechanism.

PubMed: 10631981

実験手法

X-RAY DIFFRACTION (1.81 Å)