Abstract
TOM5 is a small outer mitochondrial membrane protein in Saccharomyces cerevisiae and is part of a multi-protein translocator complex, which mediates protein import into mitochondria. Presently, nothing is known about the conformational preferences of TOM5 or other mitochondrial import proteins. In this report, circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy are used to determine the conformational preferences of the cytosolic domain of TOM5. The CD spectra show evidence of a helical structure that is invariant with pH. NOESY data revealed that TOM5 forms a stable helical core between E11 and R15 with a less structurally rigid helix extending to the C-terminus.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Biological Transport
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Circular Dichroism
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Cytosol / metabolism*
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Hydrogen-Ion Concentration
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Magnetic Resonance Spectroscopy
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Mitochondria / metabolism*
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Mitochondrial Membrane Transport Proteins*
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Mitochondrial Precursor Protein Import Complex Proteins
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Models, Molecular
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Molecular Sequence Data
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Peptide Fragments / chemistry*
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Peptide Fragments / metabolism
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Protein Structure, Secondary / physiology
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Protein Structure, Tertiary / physiology
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Saccharomyces cerevisiae
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Saccharomyces cerevisiae Proteins*
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Thiosulfate Sulfurtransferase / metabolism
Substances
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Carrier Proteins
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Membrane Proteins
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Mitochondrial Membrane Transport Proteins
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Mitochondrial Precursor Protein Import Complex Proteins
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Peptide Fragments
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Saccharomyces cerevisiae Proteins
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TOM5 protein, S cerevisiae
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Thiosulfate Sulfurtransferase