5K1S

crystal structure of AibC

5K1S の概要

• エントリーDOI: 10.2210/pdb5k1s/pdb
• 分子名称: Oxidoreductase, zinc-binding dehydrogenase family, ZINC ION (3 entities in total)
• 機能のキーワード: medium chain reductase, isovalerate, hexahistidine tag, tev-protease recognition sequence, oxidoreductase
• 由来する生物種: Myxococcus xanthus (strain DK 1622)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 153433.99

構造登録者

Bock, T.,Mueller, R.,Blankenfeldt, W. (登録日: 2016-05-18, 公開日: 2016-08-10, 最終更新日: 2024-05-08)

主引用文献

Bock, T.,Muller, R.,Blankenfeldt, W.
Crystal structure of AibC, a reductase involved in alternative de novo isovaleryl coenzyme A biosynthesis in Myxococcus xanthus.
Acta Crystallogr.,Sect.F, 72:652-658, 2016

PubMed Abstract: Isovaleryl coenzyme A (IV-CoA) performs a crucial role during development and fruiting-body formation in myxobacteria, which is reflected in the existence of a de novo biosynthetic pathway that is highly upregulated when leucine, the common precursor of IV-CoA, is limited. The final step in de novo IV-CoA biosynthesis is catalyzed by AibC, a medium-chain dehydrogenase/reductase. Here, the crystal structure of AibC from Myxococcus xanthus refined to 2.55 Å resolution is presented. The protein adopts two different conformations in the crystal lattice, which is a consequence of partial interaction with the purification tag. Based on this structure, it is suggested that AibC most probably uses a Zn(2+)-supported catalytic mechanism in which NADPH is preferred over NADH. Taken together, this study reveals structural details of the alternative IV-CoA-producing pathway in myxobacteria, which may serve as a base for further biotechnological research and biofuel production.

PubMed: 27487931
DOI: 10.1107/S2053230X16011146

実験手法

X-RAY DIFFRACTION (2.55 Å)