Structural characterization of the transmembrane segments of the mitochondrial oxoglutarate carrier (OGC) by NMR spectroscopy.
The oxoglutarate carrier (OGC) is a member of the mitochondrial carrier protein superfamily, which includes the ADP/ATP carrier and other functionally characterized members, and exchanges cytosolic malate for 2-oxoglutarate from the mitochondrial matrix. By means of CD and NMR spectroscopy, we previously characterized four synthetic peptides containing transmembrane segments (TMSs) I, II, V and VI of the OGC, respectively, in TFE/water mixtures and SDS micelles. Here, we present data on the remaining transmembrane segments of OGC obtained by performing CD and NMR studies on peptides corresponding to TMS-III and TMS-IV. In TFE/water, alpha-helical structures were found for these peptides in the L121-R146 and T187-S201 regions, respectively. We also evaluated the compatibility between the helical structures of our peptides and a homology model of the OGC based on the available X-ray structure of the ATP/ADP carrier.
Castiglione Morelli
Maria Antonietta
MA
Department of Chemistry, University of Basilicata, Potenza, Italy.
Ostuni
Angela
A
Armentano
Francesca
F
Palmieri
Ferdinando
F
Bisaccia
Faustino
F
D000818:Animals; D002417:Cattle; D002942:Circular Dichroism; D003198:Computer Simulation; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D026901:Membrane Transport Proteins / Q000737:chemistry*; D024101:Mitochondrial Proteins / Q000737:chemistry*; D008958:Models, Molecular; D017433:Protein Structure, Secondary
D026901:Membrane Transport Proteins; D024101:Mitochondrial Proteins; C021723:oxoglutarate translocator