7P9Q

Crystal structure of Indole 3-Carboxylic acid decarboxylase from Arthrobacter nicotianae FI1612 in complex with co-factor prFMN.

7P9Q の概要

• エントリーDOI: 10.2210/pdb7p9q/pdb
• 分子名称: AnInD, SODIUM ION, MANGANESE (II) ION, ... (5 entities in total)
• 機能のキーワード: anind, lyase
• 由来する生物種: Glutamicibacter nicotianae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 306229.09

構造登録者

Gahloth, D.,Leys, D. (登録日: 2021-07-27, 公開日: 2022-03-02, 最終更新日: 2024-01-31)

主引用文献

Gahloth, D.,Fisher, K.,Payne, K.A.P.,Cliff, M.,Levy, C.,Leys, D.
Structural and biochemical characterization of the prenylated flavin mononucleotide-dependent indole-3-carboxylic acid decarboxylase.
J.Biol.Chem., 298:101771-101771, 2022

PubMed Abstract: The ubiquitous UbiD family of reversible decarboxylases is implicated in a wide range of microbial processes and depends on the prenylated flavin mononucleotide cofactor for catalysis. However, only a handful of UbiD family members have been characterized in detail, and comparison between these has suggested considerable variability in enzyme dynamics and mechanism linked to substrate specificity. In this study, we provide structural and biochemical insights into the indole-3-carboxylic acid decarboxylase, representing an UbiD enzyme activity distinct from those previously studied. Structural insights from crystal structure determination combined with small-angle X-ray scattering measurements reveal that the enzyme likely undergoes an open-closed transition as a consequence of domain motion, an event that is likely coupled to catalysis. We also demonstrate that the indole-3-carboxylic acid decarboxylase can be coupled with carboxylic acid reductase to produce indole-3-carboxyaldehyde from indole + CO under ambient conditions. These insights provide further evidence for a common mode of action in the widespread UbiD enzyme family.

PubMed: 35218772
DOI: 10.1016/j.jbc.2022.101771

実験手法

X-RAY DIFFRACTION (2.53 Å)