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PDBsum entry 2c5k
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Protein transport
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PDB id
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2c5k
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References listed in PDB file
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Key reference
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Title
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Structural analysis of the interaction between the snare tlg1 and vps51.
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Authors
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Y.Fridmann-Sirkis,
H.M.Kent,
M.J.Lewis,
P.R.Evans,
H.R.Pelham.
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Ref.
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Traffic, 2006,
7,
182-190.
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PubMed id
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Abstract
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Membrane fusion in cells involves the interaction of SNARE proteins on apposing
membranes. Formation of SNARE complexes is preceded by tethering events, and a
number of protein complexes that are thought to mediate this have been
identified. The VFT or GARP complex is required for endosome-Golgi traffic in
yeast. It consists of four subunits, one of which, Vps51, has been shown to bind
specifically to the SNARE Tlg1, which participates in the same fusion event. We
have determined the structure of the N-terminal domain of Tlg1 bound to a
peptide from the N terminus of Vps51. Binding depends mainly on residues 18-30
of Vps51. These form a short helix which lies in a conserved groove in the
three-helix bundle formed by Tlg1. Surprisingly, although both Vps51 and Tlg1
are required for transport to the late Golgi from endosomes, removal of the
Tlg1-binding sequences from Vps51 does not block such traffic in vivo. Thus,
this particular interaction cannot be crucial to the process of vesicle docking
or fusion.
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