3GQ2

Crystal Structure of the Dimer of the p115 Tether Globular Head Domain

Summary for 3GQ2

• Entry DOI: 10.2210/pdb3gq2/pdb
• Descriptor: General vesicular transport factor p115 (2 entities in total)
• Functional Keywords: vesicle transport, membrane trafficking, membrane tethering, membrane fusion, snare, rab gtpase, armadillo repeats, er-golgi transport, golgi apparatus, membrane, phosphoprotein, protein transport, transport, transport protein
• Biological source: Bos taurus (bovine,cow,domestic cattle,domestic cow)
• Cellular location: Cytoplasm, cytosol: P41541
• Total number of polymer chains: 2
• Total formula weight: 145333.97

Authors

An, Y.,Elsliger, M.A.,Wilson, I.A. (deposition date: 2009-03-23, release date: 2009-11-03, Last modification date: 2024-02-21)

Primary citation

An, Y.,Chen, C.Y.,Moyer, B.,Rotkiewicz, P.,Elsliger, M.A.,Godzik, A.,Wilson, I.A.,Balch, W.E.
Structural and functional analysis of the globular head domain of p115 provides insight into membrane tethering.
J.Mol.Biol., 391:26-41, 2009

PubMed Abstract: Molecular tethers have a central role in the organization of the complex membrane architecture of eukaryotic cells. p115 is a ubiquitous, essential tether involved in vesicle transport and the structural organization of the exocytic pathway. We describe two crystal structures of the N-terminal domain of p115 at 2.0 A resolution. The p115 structures show a novel alpha-solenoid architecture constructed of 12 armadillo-like, tether-repeat, alpha-helical tripod motifs. We find that the H1 TR binds the Rab1 GTPase involved in endoplasmic reticulum to Golgi transport. Mutation of the H1 motif results in the dominant negative inhibition of endoplasmic reticulum to Golgi trafficking. We propose that the H1 helical tripod contributes to the assembly of Rab-dependent complexes responsible for the tether and SNARE-dependent fusion of membranes.

PubMed: 19414022
DOI: 10.1016/j.jmb.2009.04.062

Experimental method

X-RAY DIFFRACTION (2.18 Å)