Mitochondrial uncoupling protein 2 structure determined by NMR molecular fragment searching

Marcelo J. Berardi, William M. Shih, Stephen C. Harrison and James J. Chou ()
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Marcelo J. Berardi: Jack and Eileen Connors Structural Biology Laboratory, Harvard Medical School
William M. Shih: Harvard Medical School
Stephen C. Harrison: Jack and Eileen Connors Structural Biology Laboratory, Harvard Medical School
James J. Chou: Jack and Eileen Connors Structural Biology Laboratory, Harvard Medical School

Nature, 2011, vol. 476, issue 7358, 109-113

Abstract: Mitochondrial proton transport The transport of small molecules across the inner mitochondrial membrane is catalysed by a large family of membrane proteins called mitochondrial carriers. More than 40 different carriers have so far been identified to selectively translocate different substrates, but only one crystal structure is available — that of the bovine ADP/ATP carrier (ANT1). Now the structure of mitochondrial uncoupling protein 2 (UCP2), a member of the carrier family that translocates protons across the mitochondrial inner membrane, has been determined using a solution nuclear magnetic resonance (NMR) method. Its overall structure of resembles that of ANT1 — despite their low sequence identity — but the matrix side of the channel is substantially more open in UCP2. This method overcomes some of the challenges associated with using NMR spectroscopy to determine the structure of membrane proteins, so it seems likely that it will be possible to use the approach to solve the high-resolution NMR structures of other membrane proteins of comparable size.

Date: 2011
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DOI: 10.1038/nature10257

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