4PKF

Benzylsuccinate synthase alpha-beta-gamma complex

4PKF の概要

• エントリーDOI: 10.2210/pdb4pkf/pdb
• 関連するPDBエントリー: 4PKC
• 分子名称: TutD, TutG, TutF, ... (7 entities in total)
• 機能のキーワード: radical, complex, lyase
• 由来する生物種: Thauera aromatica; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 115949.47

構造登録者

Funk, M.A.,Drennan, C.L. (登録日: 2014-05-14, 公開日: 2014-07-02, 最終更新日: 2023-12-27)

主引用文献

Funk, M.A.,Judd, E.T.,Marsh, E.N.,Elliott, S.J.,Drennan, C.L.
Structures of benzylsuccinate synthase elucidate roles of accessory subunits in glycyl radical enzyme activation and activity.
Proc.Natl.Acad.Sci.USA, 111:10161-10166, 2014

PubMed Abstract: Anaerobic degradation of the environmental pollutant toluene is initiated by the glycyl radical enzyme benzylsuccinate synthase (BSS), which catalyzes the radical addition of toluene to fumarate, forming benzylsuccinate. We have determined crystal structures of the catalytic α-subunit of BSS with its accessory subunits β and γ, which both bind a [4Fe-4S] cluster and are essential for BSS activity in vivo. We find that BSSα has the common glycyl radical enzyme fold, a 10-stranded β/α-barrel that surrounds the glycyl radical cofactor and active site. Both accessory subunits β and γ display folds related to high potential iron-sulfur proteins but differ substantially from each other in how they interact with the α-subunit. BSSγ binds distally to the active site, burying a hydrophobic region of BSSα, whereas BSSβ binds to a hydrophilic surface of BSSα that is proximal to the active site. To further investigate the function of BSSβ, we determined the structure of a BSSαγ complex. Remarkably, we find that the barrel partially opens, allowing the C-terminal region of BSSα that houses the glycyl radical to shift within the barrel toward an exit pathway. The structural changes that we observe in the BSSαγ complex center around the crucial glycyl radical domain, thus suggesting a role for BSSβ in modulating the conformational dynamics required for enzyme activity. Accompanying proteolysis experiments support these structural observations.

PubMed: 24982148
DOI: 10.1073/pnas.1405983111

実験手法

X-RAY DIFFRACTION (2.002 Å)