PDBsum entry 3gq2

Transport protein

PDB id: 3gq2

Contents

Protein chains

614 a.a. *

Waters ×607

* Residue conservation analysis

PDB id:

3gq2

Name:

Transport protein

Title:

Crystal structure of the dimer of the p115 tether globular head domain

Structure:

General vesicular transport factor p115. Chain: a, b. Fragment: p115 tether globular head domain (unp residues 1-651). Synonym: protein uso1 homolog, transcytosis-associated protein, tap, vesicle-docking protein. Engineered: yes

Source:

Bos taurus. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913. Gene: p115, uso1, vdp. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.18Å R-factor: 0.205 R-free: 0.254

Authors:

Y.An,M.A.Elsliger,I.A.Wilson

Key ref:

Y.An et al. (2009). Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane Tethering. J Mol Biol, 391, 26-41. PubMed id: 19414022 DOI: 10.1016/j.jmb.2009.04.062

Date:

23-Mar-09 Release date: 03-Nov-09

Protein chains

P41541  (USO1_BOVIN) -  General vesicular transport factor p115 from Bos taurus

Seq: 961 a.a.

Struc: 614 a.a.

Enzyme reactions

• Enzyme class: E.C.?

DOI no: 10.1016/j.jmb.2009.04.062

J Mol Biol 391:26-41 (2009)

PubMed id: 19414022

Structural and Functional Analysis of the Globular Head Domain of p115 Provides Insight into Membrane Tethering.

Y.An, C.Y.Chen, B.Moyer, P.Rotkiewicz, M.A.Elsliger, A.Godzik, I.A.Wilson, W.E.Balch.

ABSTRACT

Molecular tethers play 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 (TR), alpha-helical tripod motifs. We find that the H1 TR binds the Rab1 GTPase involved in ER to Golgi transport. Mutation of the H1 motif results in the dominant negative inhibition of ER 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.

Selected figure(s)

Figure 2.
Fig. 2. Salt bridges and hydrogen bond interactions involved in p115^Nt dimerization. Hydrogen bonds and salt bridges are shown as broken lines, with interacting residues in ball-and-stick representation.

Figure 3.
Fig. 3. Tether repeat (TR) motif. (a) Structural features of the 12 TRs in the p115^Nt monomer. Except for the C-terminal TR, each TR includes three α-helices, which are shown in salmon, yellow and light blue, respectively. The insertions between any adjacent helices are colored gray. Arg39 is shown in ball-and-stick representation; the side view is in the left-hand panel, and the top view is in the right-hand panel. (b) The conformation of three adjacent tether repeats (TR5, TR6, and TR7) highlights the tight packing of the conserved hydrophobic core throughout the solenoid, where the hydrophobic residues involved in stabilizing the solenoid are shown in ball-and-stick representation. (c) Superimposition of the three 12 TR motifs from the dimer and monomer p115^Nt structures show the structural conservation.

The above figures are reprinted by permission from Elsevier: J Mol Biol (2009, 391, 26-41) copyright 2009.

Figures were selected by an automated process.