262
Views
6
CrossRef citations to date
0
Altmetric
Original

Solution structure of the fifth and sixth transmembrane segments of the mitochondrial oxoglutarate carrier

, , , &
Pages 191-201 | Received 23 Sep 2004, Published online: 09 Jul 2009

References

  • Bax A, Davis DG. MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy. J Magn Reson 1985; 65: 355–366
  • Bhattacharyya R, Chakrabarti P. Stereospecific interactions of proline residues in protein structures and complexes. J Mol Biol 2003; 331: 925–940
  • Bisaccia F, Capobianco L, Brandolin G, Palmieri F. Transmembrane topography of the mitochondrial oxoglutarate carrier assessed by peptide-specific antibodies and enzymatic cleavage. Biochemistry 1994; 33: 3705–3713
  • Bisaccia F, Zara V, Capobianco L, Iacobazzi V, Mazzeo M, Palmieri F. The formation of a disulfide cross-link between the two subunits demonstrates the dimeric structure of the mitochondrial oxoglutarate carrier. Biochim Biophys Acta 1996; 1292: 281–288
  • Bywater RP, Thomas D, Vriend G. A sequence and structural study of transmembrane helices. J Comput Aided Mol Des 2001; 15: 533–552
  • Buck M. Trifluoroethanol and colleagues: Cosolvents come of age. Recent studies with peptides and proteins. Q Rev Biophys 1998; 31: 297–355
  • Castiglione Morelli MA, Ostuni A, Pepe A, Lauria G, Palmieri F, Bisaccia F. Solution structure of the first and second transmembrane segments of the mitochondrial oxoglutarate carrier. Mol Membr Biol 2004; 21: 297–305
  • Chopra A, Yeagle PL, Alderfer JL, Albert AD. Solution structure of the sixth transmembrane helix of the G-protein-coupled receptor, rhodopsin. Biochim Biophys Acta 2000; 1463: 1–5
  • Chou PY, Fasman GD. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry 1974; 13: 211–222
  • Deléage G, Clerc FF, Roux B, Gautheron DC. ANTHEPROT: A package for protein sequence analysis using a microcomputer. Comput Appl Biosci 1988; 4: 351–356
  • Guntert P, Mumenthaler M, Wüthrich K. Torsion angle dynamics for NMR structure calculation with the new program DYANA. J Mol Biol 1997; 273: 283–298
  • Jeener J, Meier BH, Bachmann P, Ernst RR. Investigation of exchange processes by two-dimensional NMR spectroscopy. J Chem Phys 1979; 71: 4546–4553
  • Katragadda M, Alderfer JL, Yeagle PL. Solution structure of the loops of bacteriorhodopsin closely resembles the crystal structure. Biochim Biophys Acta 2000; 1466: 1–6
  • Katragadda M, Alderfer JL, Yeagle PL. Assembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin. Biophys J 2001; 81: 1029–1036
  • King DS, Fields CG, Fields GB. A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis. Int J Peptide Protein Res 1990; 36: 255–266
  • Koradi R, Billeter M, Wüthrich K. MOLMOL: A program for display and analysis of macromolecular structures. J Mol Graphics 1996; 14: 51–55
  • Krämer R, Palmieri F. Metabolite carriers in mitochondria. Molecular mechanisms in bioenergetics, L Ernster. Elsevier Science BV, Amsterdam 1992; 359–384
  • Merutka G, Dyson HJ, Wright PE. ‘Random coil’ 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG. J Biomol NMR 1995; 5: 14–24
  • Morozzo della Rocca B, Lauria G, Venerini F, Palmieri L, Polizio F, Capobianco L, Stipani V, Pedersen J, Cappello AR, Desideri A, Palmieri F. The mitochondrial oxoglutarate carrier: Structural and dynamic properties of transmembrane segment IV studied by site-directed spin labelling. Biochemistry 2003; 42: 5493–5499
  • Palmieri F. Mitochondrial carrier proteins. FEBS Lett 1994; 346: 48–54
  • Palmieri F, Bisaccia F, Capobianco L, Dolce V, Fiermonte G, Iacobazzi V, Indiveri C, Palmieri L. Mitochondrial metabolite transporters. Biochim Biophys Acta 1996; 1275: 127–132
  • Palmieri F. The ABC of solute carriers. Pflugers Arch Europ J Physiol 2004; 447: 689–709
  • Pearce SF, Hawrot E. Intrinsic fluorescence of binding-site fragments of the nicotinic acetylcholine receptor: Perturbations produced upon binding α-bungrotoxin. Biochemistry 1990; 29: 10649–10659
  • Pebay-Peyroula CE, Dahou-Gonzales C, Kahn R, Trezeguet V, Lauquin GJM, Brandolin G. Structure of mitochondrial ADP/ATP carrier in complex with carboxyatractyloside. Nature 2003; 426: 39–43
  • Piantini U, Sorensen OW, Ernst RR. Multiple quantum filters for elucidating NMR coupling networks. J Am Chem 1982; 169: 949–961
  • Piotto M, Saudek V, Sklenar V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 1992; 2: 661–665
  • Raussens V, Slupsky CM, Ryan RO, Sykes BD. NMR structure and dynamics of a receptor-active apolipoprotein E peptide. J Biol Chem 2002; 277: 29172–29180
  • Richardson JS, Richardson DC. Amino acid preferences for specific locations at the ends of α-helices. Science 1988; 240: 1648–1652
  • Runswich MJ, Walker JE, Bisaccia F, Iacobazzi V, Palmieri F. Sequence of the bovine 2-oxoglutarate/malate carrier protein: Structural relationship to other mitochondrial transport proteins. Biochemistry 1990; 29: 11033–11040
  • Sreerama N, Woody RW. Circular dichroism of peptides and proteins. Circular dichroism: principles and applications, N Berova, K Nakanishi, RW Woody. Wiley, New York 2000; 601–620
  • States DJ, Haberkorn RA, Ruben DJ. A two-dimensional nuclear Overhauser experiment with pure absorption phase in four quadrants. J Magn Reson 1982; 48: 286–292
  • Stipani V, Cappello AR, Daddabbo L, Natuzzi D, Miniero DV, Stipani I, Palmieri F. The mitochondrial oxoglutarate carrier: cysteine-scanning mutagenesis of transmembrane domain IV and sensitivity of Cys mutants to sulfhydryl reagents. Biochemistry 2001; 40: 15805–15810
  • von Heijne G. Proline kinks in transmembrane α-helices. J Mol Biol 1991; 218: 499–503
  • Walker JE, Runswick MJ. The mitochondrial protein superfamily. J Bioenerg Biomembr 1993; 25: 435–446
  • Wishart DS, Sykes BD, Richards FM. Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J Mol Biol 1991; 222: 311–333
  • Wüthrich K, Billeter M, Braun W. Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance. J Mol Biol 1983; 169: 949–961
  • Wüthrich K. NMR of proteins and nucleic acids. Wiley, New York 1986

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.