2c5i
N-TERMINAL DOMAIN OF TLG1 COMPLEXED WITH N-TERMINUS OF VPS51 IN DISTORTED CONFORMATION
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OverviewOverview
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, ... [(full description)]
About this StructureAbout this Structure
2C5I is a [Protein complex] structure of sequences from [Saccharomyces cerevisiae] with SO4 as [ligand]. Full crystallographic information is available from [OCA].
ReferenceReference
Structural analysis of the interaction between the SNARE Tlg1 and Vps51., Fridmann-Sirkis Y, Kent HM, Lewis MJ, Evans PR, Pelham HR, Traffic. 2006 Feb;7(2):182-90. PMID:16420526
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