2C5I

N-terminal domain of tlg1 complexed with N-terminus of vps51 in distorted conformation

Summary for 2C5I

• Entry DOI: 10.2210/pdb2c5i/pdb
• Related: 2C5J 2C5K
• Descriptor: VACUOLAR PROTEIN SORTING PROTEIN 51, T-SNARE AFFECTING A LATE GOLGI COMPARTMENT PROTEIN 1, SULFATE ION, ... (4 entities in total)
• Functional Keywords: protein transport-complex, snare, vft complex, protein transport, phosphorylation
• Biological source: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); More
• Cellular location: Golgi apparatus, trans-Golgi network membrane; Single-pass type IV membrane protein (Probable): Q03322; Golgi apparatus, trans-Golgi network membrane; Peripheral membrane protein: P36116
• Total number of polymer chains: 2
• Total formula weight: 15632.01

Authors

Fridmann-Sirkis, Y.,Kent, H.M.,Lewis, M.J.,Evans, P.R.,Pelham, H.R.B. (deposition date: 2005-10-27, release date: 2006-01-25, Last modification date: 2024-10-16)

Primary citation

Fridmann-Sirkis, Y.,Kent, H.M.,Lewis, M.J.,Evans, P.R.,Pelham, H.R.B.
Structural Analysis of the Interaction between the Snare Tlg1 and Vps51.
Traffic, 7:182-, 2006

PubMed Abstract: 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.

PubMed: 16420526
DOI: 10.1111/J.1600-0854.2005.00374.X

Experimental method

X-RAY DIFFRACTION (2.3 Å)