Chrysler Navtec 05064033ai Inmotion 2 15 32 Iso





 
 
 
 
 
 
 

Chrysler Navtec 05064033ai Inmotion 2 15 32 Iso

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chrysler navtec 05064033ai inmotion 2 15 32 iso,chrysler navtec 05064033ai inmotion 2 15 32 iso,download chrysler navtec 05064033ai inmotion 2 15 32 iso,Structure of the mitochondrial carboxylate carrier (SLC25A1) complexed with isobutyric acid: implications for proton binding in the transport reaction.
SLC25A1, the mammalian isoform of the yeast mitochondrial carriers, serves as an ion-coupled electrogenic exchanger for dicarboxylates and as a proton carrier for acyl-coenzyme A. The X-ray crystal structure of the complex of SLC25A1 with isobutyric acid (IBA) at 2.3-A resolution reveals a trimer in the asymmetric unit with a three-fold helical symmetry axis. Each protomer consists of a long N-terminal alpha-helix of 24 residues, a larger central alpha-helix of 57 residues, and a smaller C-terminal alpha-helix of 34 residues. In the asymmetric unit, three protein molecules are arranged in a trimer of dimers with a pseudo-twofold axis of 42.5 degrees. Amino acids at the two interprotomer interfaces contribute ion pairs to the binding site for IBA and regulate the transporter-mediated transport activity. The substrate-binding site of SLC25A1 contains two long parallel alpha-helices forming a trifurcated cap and a highly curved hydrophilic channel running parallel to the helical axes. The cap and channel form a D-like shape with a width of 10 A that can accommodate a substrate. The two beta-barrels

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