4MTU

beta-Alanyl-CoA:Ammonia Lyase from Clostridium propionicum

4MTU の概要

• エントリーDOI: 10.2210/pdb4mtu/pdb
• 関連するPDBエントリー: 4MZQ
• 分子名称: Beta-alanyl-CoA:ammonia lyase 2, ZINC ION, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: hot dog fold, lyase
• 由来する生物種: Clostridium propionicum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16185.67

構造登録者

Heine, A.,Reuter, K. (登録日: 2013-09-20, 公開日: 2014-03-26, 最終更新日: 2024-02-28)

主引用文献

Heine, A.,Herrmann, G.,Selmer, T.,Terwesten, F.,Buckel, W.,Reuter, K.
High resolution crystal structure of Clostridium propionicum beta-alanyl-CoA:ammonia lyase, a new member of the "hot dog fold" protein superfamily.
Proteins, 82:2041-2053, 2014

PubMed Abstract: Clostridium propionicum is the only organism known to ferment β-alanine, a constituent of coenzyme A (CoA) and the phosphopantetheinyl prosthetic group of holo-acyl carrier protein. The first step in the fermentation is a CoA-transfer to β-alanine. Subsequently, the resulting β-alanyl-CoA is deaminated by the enzyme β-alanyl-CoA:ammonia lyase (Acl) to reversibly form ammonia and acrylyl-CoA. We have determined the crystal structure of Acl in its apo-form at a resolution of 0.97 Å as well as in complex with CoA at a resolution of 1.59 Å. The structures reveal that the enyzme belongs to a superfamily of proteins exhibiting a so called "hot dog fold" which is characterized by a five-stranded antiparallel β-sheet with a long α-helix packed against it. The functional unit of all "hot dog fold" proteins is a homodimer containing two equivalent substrate binding sites which are established by the dimer interface. In the case of Acl, three functional dimers combine to a homohexamer strongly resembling the homohexamer formed by YciA-like acyl-CoA thioesterases. Here, we propose an enzymatic mechanism based on the crystal structure of the Acl·CoA complex and molecular docking.

PubMed: 24623648
DOI: 10.1002/prot.24557

実験手法

X-RAY DIFFRACTION (0.97 Å)