2GPW

Crystal Structure of the Biotin Carboxylase Subunit, F363A Mutant, of Acetyl-CoA Carboxylase from Escherichia coli.

2GPW の概要

• エントリーDOI: 10.2210/pdb2gpw/pdb
• 関連するPDBエントリー: 1bnc 1dv1 1dv2 1w93 1w96
• 分子名称: Biotin carboxylase (2 entities in total)
• 機能のキーワード: atp-grasp, carboxylase, biotin-dependent, fatty acid synthesis, dimer-interface mutant, ligase
• 由来する生物種: Escherichia coli
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 205927.69

構造登録者

Shen, Y.,Chou, C.Y.,Chang, G.G.,Tong, L. (登録日: 2006-04-18, 公開日: 2006-07-04, 最終更新日: 2023-08-30)

主引用文献

Shen, Y.,Chou, C.Y.,Chang, G.G.,Tong, L.
Is dimerization required for the catalytic activity of bacterial biotin carboxylase?
Mol.Cell, 22:807-818, 2006

PubMed Abstract: Acetyl-coenzyme A carboxylases (ACCs) have crucial roles in fatty acid metabolism. The biotin carboxylase (BC) subunit of Escherichia coli ACC is believed to be active only as a dimer, although the crystal structure shows that the active site of each monomer is 25 A from the dimer interface. We report here biochemical, biophysical, and structural characterizations of BC carrying single-site mutations in the dimer interface. Our studies demonstrate that two of the mutants, R19E and E23R, are monomeric in solution but have only a 3-fold loss in catalytic activity. The crystal structures of the E23R and F363A mutants show that they can still form the correct dimer at high concentrations. Our data suggest that dimerization is not an absolute requirement for the catalytic activity of the E. coli BC subunit, and we propose a new model for the molecular mechanism of action for BC in multisubunit and multidomain ACCs.

PubMed: 16793549
DOI: 10.1016/j.molcel.2006.04.026

実験手法

X-RAY DIFFRACTION (2.2 Å)