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Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers.

H Nury¹, C Dahout-Gonzalez, V Trézéguet

¹Institut de Biologie Structurale, UMR 5075 CEA-CNRS-Université Joseph Fourier, F-38027 Grenoble Cedex 1, France.

|October 18, 2005

Summary

The ADP/ATP carrier

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Area of Science:

Mitochondrial biology
Structural biology
Biochemistry

Background:

The ADP/ATP carrier (AAC) is crucial for energy metabolism, facilitating nucleotide exchange across the inner mitochondrial membrane.
Understanding AAC's oligomerization state is key to elucidating its transport mechanism.
Previous structural studies revealed inhibitor binding within a monomeric cavity, with non-biologically relevant interactions.

Purpose of the Study:

To investigate the biologically relevant oligomerization state of the ADP/ATP carrier.
To characterize protein-protein interactions mediated by endogenous lipids.

Main Methods:

X-ray crystallography of the ADP/ATP carrier.
Analysis of protein-lipid interactions.

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Main Results:

A new crystal form of the ADP/ATP carrier was determined, revealing biologically relevant protein-protein interactions.
Endogenous cardiolipins mediate these interactions, with two cardiolipin molecules positioned between monomers.
A putative dimerization interface was identified, supported by existing data.

Conclusions:

The ADP/ATP carrier likely functions as a dimer in its biologically active state.
Cardiolipin plays a critical role in stabilizing the dimeric structure of the ADP/ATP carrier.
These findings provide structural insights into the mechanism of mitochondrial nucleotide transport.