6NS5

Crystal structure of fungal lipoxygenase from Fusarium graminearum. Second C2 crystal form.

6NS5 の概要

• エントリーDOI: 10.2210/pdb6ns5/pdb
• 関連するPDBエントリー: 6NS2 6NS3 6NS4 6NS6
• 分子名称: lipoxygenase, FE (II) ION (3 entities in total)
• 機能のキーワード: lipoxygenase, fungus, fe coordination, oxidoreductase
• 由来する生物種: Gibberella zeae (strain PH-1 / ATCC MYA-4620 / FGSC 9075 / NRRL 31084) (Wheat head blight fungus)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 172925.22

構造登録者

Pakhomova, S.,Boeglin, W.E.,Neau, D.B.,Bartlett, S.G.,Brash, A.R.,Newcomer, M.E. (登録日: 2019-01-24, 公開日: 2019-03-27, 最終更新日: 2023-10-11)

主引用文献

Pakhomova, S.,Boeglin, W.E.,Neau, D.B.,Bartlett, S.G.,Brash, A.R.,Newcomer, M.E.
An ensemble of lipoxygenase structures reveals novel conformations of the Fe coordination sphere.
Protein Sci., 28:920-927, 2019

PubMed Abstract: The regio- and stereo-specific oxygenation of polyunsaturated fatty acids is catalyzed by lipoxygenases (LOX); both Fe and Mn forms of the enzyme have been described. Structural elements of the Fe and Mn coordination spheres and the helical catalytic domain in which the metal center resides are highly conserved. However, animal, plant, and microbial LOX each have distinct features. We report five crystal structures of a LOX from the fungal plant pathogen Fusarium graminearum. This LOX displays a novel amino terminal extension that provides a wrapping domain for dimerization. Moreover, this extension appears to interfere with the iron coordination sphere, as the typical LOX configuration is not observed at the catalytic metal when the enzyme is dimeric. Instead novel tetra-, penta-, and hexa-coordinate Fe ligations are apparent. In contrast, a monomeric structure indicates that with repositioning of the amino terminal segment, the enzyme can assume a productive conformation with the canonical Fe coordination sphere.

PubMed: 30861228
DOI: 10.1002/pro.3602

実験手法

X-RAY DIFFRACTION (2.79 Å)