7NUJ

Crystal structure of holo-SwHPA-Mg (hydroxy ketone aldolase) from Sphingomonas wittichii RW1

7NUJ の概要

• エントリーDOI: 10.2210/pdb7nuj/pdb
• 関連するPDBエントリー: 6R62 7NNK 7NR1
• 分子名称: HpcH/HpaI aldolase, MAGNESIUM ION (3 entities in total)
• 機能のキーワード: class ii pyruvate aldolase, metal dependent aldolase, aldol reaction, magnesium, carbon bond formation, lyase
• 由来する生物種: Sphingomonas wittichii RW1
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 53617.66

構造登録者

Laustsen, J.,Justo, I.,Marsden, S.R.,Hanefeld, U.,Bento, I. (登録日: 2021-03-12, 公開日: 2022-09-21, 最終更新日: 2024-01-31)

主引用文献

Marsden, S.R.,Wijma, H.J.,Mohr, M.K.F.,Justo, I.,Hagedoorn, P.L.,Laustsen, J.,Jeffries, C.M.,Svergun, D.,Mestrom, L.,McMillan, D.G.G.,Bento, I.,Hanefeld, U.
Substrate Induced Movement of the Metal Cofactor between Active and Resting State.
Angew.Chem.Int.Ed.Engl., 61:e202213338-e202213338, 2022

PubMed Abstract: Regulation of enzyme activity is vital for living organisms. In metalloenzymes, far-reaching rearrangements of the protein scaffold are generally required to tune the metal cofactor's properties by allosteric regulation. Here structural analysis of hydroxyketoacid aldolase from Sphingomonas wittichii RW1 (SwHKA) revealed a dynamic movement of the metal cofactor between two coordination spheres without protein scaffold rearrangements. In its resting state configuration (M ), the metal constitutes an integral part of the dimer interface within the overall hexameric assembly, but sterical constraints do not allow for substrate binding. Conversely, a second coordination sphere constitutes the catalytically active state (M ) at 2.4 Å distance. Bidentate coordination of a ketoacid substrate to M affords the overall lowest energy complex, which drives the transition from M to M . While not described earlier, this type of regulation may be widespread and largely overlooked due to low occupancy of some of its states in protein crystal structures.

PubMed: 36214476
DOI: 10.1002/anie.202213338

実験手法

X-RAY DIFFRACTION (1.9 Å)