1NVM

Crystal structure of a bifunctional aldolase-dehydrogenase : sequestering a reactive and volatile intermediate

1NVM の概要

• エントリーDOI: 10.2210/pdb1nvm/pdb
• 分子名称: 4-hydroxy-2-oxovalerate aldolase, acetaldehyde dehydrogenase (acylating), MANGANESE (II) ION, ... (8 entities in total)
• 機能のキーワード: sequestered tunnel, substrate channeling, bifunctional enzyme, lyase-oxidoreductase complex, lyase/oxidoreductase
• 由来する生物種: Pseudomonas sp.; 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 285361.73

構造登録者

Manjasetty, A.B.,Powlowski, J.,Vrielink, A. (登録日: 2003-02-04, 公開日: 2003-06-17, 最終更新日: 2024-02-14)

主引用文献

Manjasetty, A.B.,Powlowski, J.,Vrielink, A.
Crystal structure of a bifunctional aldolase-dehydrogenase: Sequestering a reactive and volatile intermediate
Proc.Natl.Acad.Sci.USA, 100:6992-6997, 2003

PubMed Abstract: The crystal structure of the bifunctional enzyme 4-hydroxy-2-ketovalerate aldolase (DmpG)/acylating acetaldehyde dehydrogenase (DmpF), which is involved in the bacterial degradation of toxic aromatic compounds, has been determined by multiwavelength anomalous dispersion (MAD) techniques and refined to 1.7-A resolution. Structures of the two polypeptides represent a previously unrecognized subclass of metal-dependent aldolases, and of a CoA-dependent dehydrogenase. The structure reveals a mixed state of NAD+ binding to the DmpF protomer. Domain movements associated with cofactor binding in the DmpF protomer may be correlated with channeling and activity at the DmpG protomer. In the presence of NAD+ a 29-A-long sequestered tunnel links the two active sites. Two barriers are visible along the tunnel and suggest control points for the movement of the reactive and volatile acetaldehyde intermediate between the two active sites.

PubMed: 12764229
DOI: 10.1073/pnas.1236794100

実験手法

X-RAY DIFFRACTION (1.7 Å)