2c5j | pdb_00002c5j

N-TERMINAL DOMAIN OF TLG1, DOMAIN-SWAPPED DIMER

spinqualitylabelsall models 2c5j, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2c5j is a 2 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2c5i, 2c5k Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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