Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching

Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching Mitochondrial uncoupling protein 2 (UCP2) is an integral membrane protein in the mitochondrial anion carrier protein family, the members of which facilitate the transport of small molecules across the mitochondrial inner membrane . When the mitochondrial respiratory complex pumps protons from the mitochondrial matrix to the intermembrane space, it builds up an electrochemical potential . A fraction of this electrochemical potential is dissipated as heat, in a process involving leakage of protons back to the matrix . This leakage, or ‘uncoupling’ of the proton electrochemical potential, is mediated primarily by uncoupling proteins . However, the mechanism of UCP-mediated proton translocation across the lipid bilayer is unknown. Here we describe a solution-NMR method for structural characterization of UCP2. The method, which overcomes some of the challenges associated with membrane-protein structure determination , combines orientation restraints derived from NMR residual dipolar couplings (RDCs) and semiquantitative distance restraints from paramagnetic relaxation enhancement (PRE) measurements. The local and secondary structures of the protein were determined by piecing together molecular fragments from the Protein Data Bank that best fit experimental RDCs from samples weakly aligned in a DNA nanotube liquid crystal. The RDCs also determine the relative orientation of the secondary structural segments, http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Nature Nature Publishing Group (NPG)

Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching

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Publisher
Nature Publishing Group (NPG)
Copyright
Copyright © 2011 Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved.
ISSN
0028-0836
eISSN
1476-4687
D.O.I.
10.1038/nature10257
Publisher site
See Article on Publisher Site

Abstract

Mitochondrial uncoupling protein 2 (UCP2) is an integral membrane protein in the mitochondrial anion carrier protein family, the members of which facilitate the transport of small molecules across the mitochondrial inner membrane . When the mitochondrial respiratory complex pumps protons from the mitochondrial matrix to the intermembrane space, it builds up an electrochemical potential . A fraction of this electrochemical potential is dissipated as heat, in a process involving leakage of protons back to the matrix . This leakage, or ‘uncoupling’ of the proton electrochemical potential, is mediated primarily by uncoupling proteins . However, the mechanism of UCP-mediated proton translocation across the lipid bilayer is unknown. Here we describe a solution-NMR method for structural characterization of UCP2. The method, which overcomes some of the challenges associated with membrane-protein structure determination , combines orientation restraints derived from NMR residual dipolar couplings (RDCs) and semiquantitative distance restraints from paramagnetic relaxation enhancement (PRE) measurements. The local and secondary structures of the protein were determined by piecing together molecular fragments from the Protein Data Bank that best fit experimental RDCs from samples weakly aligned in a DNA nanotube liquid crystal. The RDCs also determine the relative orientation of the secondary structural segments,

Journal

NatureNature Publishing Group (NPG)

Published: Jul 24, 2011

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