2C5I: N-Terminal Domain Of Tlg1 Complexed With N-Terminus Of Vps51 In Distorted Conformation

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.
PDB ID: 2C5IDownload
MMDB ID: 86900
PDB Deposition Date: 2005/10/27
Updated in MMDB: 2010/12
Experimental Method:
x-ray diffraction
Resolution: 2.3  Å
Source Organism:
Similar Structures:
Biological Unit for 2C5I: dimeric; determined by author and by software (PQS)
Molecular Components in 2C5I
Label Count Molecule
Proteins (2 molecules)
T-snare Affecting a Late Golgi Compartment Protein 1(Gene symbol: TLG1)
Molecule annotation
Vacuolar Protein Sorting Protein 51(Gene symbol: VPS51)
Molecule annotation
Chemical (1 molecule)
* Click molecule labels to explore molecular sequence information.

Citing MMDB