6LQ4

Crystal Structure of E447A Acyl-CoA Dehydrogenase FadE5 mutant from Mycobacteria smegmatis in complex with C14CoA

Summary for 6LQ4

• Entry DOI: 10.2210/pdb6lq4/pdb
• Descriptor: Acyl-CoA dehydrogenase, FLAVIN-ADENINE DINUCLEOTIDE, MYRISTIC ACID, ... (5 entities in total)
• Functional Keywords: dehydrogenase, oxidoreductase
• Biological source: Mycobacterium smegmatis
• Total number of polymer chains: 2
• Total formula weight: 136649.32

Authors

Liu, X.,Chen, X.B. (deposition date: 2020-01-13, release date: 2020-07-01, Last modification date: 2024-03-27)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (2.4 Å)