6KSB

Crystal Structure of E447A M130G Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C16CoA

6KSB の概要

• エントリーDOI: 10.2210/pdb6ksb/pdb
• 分子名称: Acyl-CoA dehydrogenase, GLYCEROL, FLAVIN-ADENINE DINUCLEOTIDE, ... (6 entities in total)
• 機能のキーワード: fade5, oxidoreductase
• 由来する生物種: Mycobacterium smegmatis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 136741.33

構造登録者

Liu, X.,Chen, X.B. (登録日: 2019-08-23, 公開日: 2020-07-01, 最終更新日: 2024-03-27)

主引用文献

Chen, X.,Chen, J.,Yan, B.,Zhang, W.,Guddat, L.W.,Liu, X.,Rao, Z.
Structural basis for the broad substrate specificity of two acyl-CoA dehydrogenases FadE5 from mycobacteria.
Proc.Natl.Acad.Sci.USA, 117:16324-16332, 2020

PubMed Abstract: FadE, an acyl-CoA dehydrogenase, introduces unsaturation to carbon chains in lipid metabolism pathways. Here, we report that FadE5 from (FadE5) and (FadE5) play roles in drug resistance and exhibit broad specificity for linear acyl-CoA substrates but have a preference for those with long carbon chains. Here, the structures of FadE5 and FadE5, in the presence and absence of substrates, have been determined. These reveal the molecular basis for the broad substrate specificity of these enzymes. FadE5 interacts with the CoA region of the substrate through a large number of hydrogen bonds and an unusual π-π stacking interaction, allowing these enzymes to accept both short- and long-chain substrates. Residues in the substrate binding cavity reorient their side chains to accommodate substrates of various lengths. Longer carbon-chain substrates make more numerous hydrophobic interactions with the enzyme compared with the shorter-chain substrates, resulting in a preference for this type of substrate.

PubMed: 32601219
DOI: 10.1073/pnas.2002835117

実験手法

X-RAY DIFFRACTION (1.973 Å)