Abstract
Ykt6p is a nonsyntaxin SNARE implicated in multiple intracellular membrane trafficking steps. Here we present the structure of the NH2-terminal domain of Ykt6p (Ykt6pN, residues 1 to 140). The structure of Ykt6pN differed entirely from that of syntaxin and resembled the overall fold of the actin regulatory protein, profilin. Like some syntaxins, Ykt6p adopted a folded back conformation in which Ykt6pN bound to its COOH-terminal core domain. The NH2-terminal domain plays an important biological role in the function of Ykt6p, which in vitro studies revealed to include influencing the kinetics and proper assembly of SNARE complexes.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Carrier Proteins / chemistry*
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Carrier Proteins / metabolism
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Contractile Proteins*
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Membrane Proteins / chemistry*
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Membrane Proteins / metabolism
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Microfilament Proteins / chemistry
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Models, Molecular
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Molecular Sequence Data
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Molecular Weight
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Mutagenesis
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Nuclear Magnetic Resonance, Biomolecular
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Profilins
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Protein Binding
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Protein Conformation
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Protein Folding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Qa-SNARE Proteins
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Qc-SNARE Proteins
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R-SNARE Proteins
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Recombinant Fusion Proteins / chemistry
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Recombinant Fusion Proteins / metabolism
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SNARE Proteins
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Saccharomyces cerevisiae Proteins*
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Vesicular Transport Proteins*
Substances
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Carrier Proteins
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Contractile Proteins
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Membrane Proteins
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Microfilament Proteins
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Profilins
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Qa-SNARE Proteins
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Qc-SNARE Proteins
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R-SNARE Proteins
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Recombinant Fusion Proteins
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SFT1 protein, S cerevisiae
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SNARE Proteins
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Saccharomyces cerevisiae Proteins
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Sed5 protein, S cerevisiae
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Vesicular Transport Proteins
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YKT6 protein, S cerevisiae