3GF3

Glutaconyl-coA decarboxylase A subunit from Clostridium symbiosum co-crystallized with glutaconyl-coA

3GF3 の概要

• エントリーDOI: 10.2210/pdb3gf3/pdb
• 関連するPDBエントリー: 3GF7 3GLM 3GMA
• 分子名称: Glutaconyl-CoA decarboxylase subunit A, CROTONYL COENZYME A, CHLORIDE ION, ... (4 entities in total)
• 機能のキーワード: glutaconyl-coa decarboxylase, sodium ion transport, biotin, glutamate fermentation, lyase
• 由来する生物種: Clostridium symbiosum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 65895.04

構造登録者

Kress, D.,Brugel, D.,Buckel, W.,Essen, L.-O. (登録日: 2009-02-26, 公開日: 2009-07-28, 最終更新日: 2023-11-01)

主引用文献

Kress, D.,Brugel, D.,Schall, I.,Linder, D.,Buckel, W.,Essen, L.-O.
An asymmetric model for Na+-translocating glutaconyl-CoA decarboxylases
J.Biol.Chem., 284:28401-28409, 2009

PubMed Abstract: Glutaconyl-CoA decarboxylase (Gcd) couples the biotin-dependent decarboxylation of glutaconyl-CoA with the generation of an electrochemical Na(+) gradient. Sequencing of the genes encoding all subunits of the Clostridium symbiosum decarboxylase membrane complex revealed that it comprises two distinct biotin carrier subunits, GcdC(1) and GcdC(2), which differ in the length of a central alanine- and proline-rich linker domain. Co-crystallization of the decarboxylase subunit GcdA with the substrate glutaconyl-CoA, the product crotonyl-CoA, and the substrate analogue glutaryl-CoA, respectively, resulted in a high resolution model for substrate binding and catalysis revealing remarkable structural changes upon substrate binding. Unlike the GcdA structure from Acidaminococcus fermentans, these data suggest that in intact Gcd complexes, GcdA is associated as a tetramer crisscrossed by a network of solvent-filled tunnels.

PubMed: 19654317
DOI: 10.1074/jbc.M109.037762

実験手法

X-RAY DIFFRACTION (1.75 Å)