%0 Journal Article
%T NMR Characterization of Long-Chain Fatty Acylcarnitine Binding to the Mitochondrial Carnitine/Acylcarnitine Carrier.
%A Zhang N
%A Jia X
%A Fan S
%A Wu B
%A Wang S
%A OuYang B
%A Zhang N
%A Jia X
%A Fan S
%A Wu B
%A Wang S
%A OuYang B
%A Zhang N
%A Jia X
%A Fan S
%A Wu B
%A Wang S
%A OuYang B
%A Zhang N
%A Jia X
%A Fan S
%A Wu B
%A Wang S
%A OuYang B
%J Int J Mol Sci
%V 23
%N 9
%D Apr 2022 21
%M 35563000
%F 6.208
%R 10.3390/ijms23094608
%X The mitochondrial carnitine/acylcarnitine carrier (CAC) transports short-, medium- and long-carbon chain acylcarnitines across the mitochondrial inner membrane in exchange for carnitine. How CAC recognizes the substrates with various fatty acyl groups, especially long-chain fatty acyl groups, remains unclear. Here, using nuclear magnetic resonance (NMR) technology, we have shown that the CAC protein reconstituted into a micelle system exhibits a typical six transmembrane structure of the mitochondrial carrier family. The chemical shift perturbation patterns of different fatty acylcarnitines suggested that the segment A76-G81 in CAC specifically responds to the long-chain fatty acylcarnitine. Molecular dynamics (MD) simulations of palmitoyl-L-carnitine inside the CAC channel showed the respective interaction and motion of the long-chain acylcarnitine in CAC at the cytosol-open state and matrix-open state. Our data provided a molecular-based understanding of CAC structure and transport mechanism.