PDBsum entry 3etu

Transport protein

PDB id

3etu

Loading ...

Contents

			Protein chain

					313 a.a.

			Waters ×49

PDB id:

3etu

Links

Name:

Transport protein

Title:

Crystal structure of yeast dsl1p

Structure:

Protein transport protein dsl1. Chain: a. Fragment: n-terminal fragment (unp residues 1-361). Synonym: dependent on sly1-20 protein 1. Engineered: yes

Source:

Saccharomyces cerevisiae. Yeast. Organism_taxid: 4932. Gene: dsl1, n0842, ynl258c. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

2.40Å

R-factor:

0.231

R-free:

0.266

Authors:

Y.Ren,P.D.Jeffrey,F.M.Hughson

Key ref:

A.Tripathi et al. (2009). Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nat Struct Biol, 16, 114-123. PubMed id: 19151722

Date:

08-Oct-08

Release date:

20-Jan-09

PROCHECK

	Headers

	References

Protein chain

P53847 (DSL1_YEAST) - Protein transport protein DSL1 from Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

Seq: Struc:

Seq: Struc:					754 a.a. 313 a.a.

Key:

PfamA domain

Secondary structure

CATH domain

	Nat Struct Biol 16:114-123 (2009)
PubMed id: 19151722

Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex.
A.Tripathi, Y.Ren, P.D.Jeffrey, F.M.Hughson.

ABSTRACT

Multisubunit tethering complexes are essential for intracellular trafficking and have been proposed to mediate the initial interaction between vesicles and the membranes with which they fuse. Here we report initial structural characterization of the Dsl1p complex, whose three subunits are essential for trafficking from the Golgi apparatus to the endoplasmic reticulum (ER). Crystal structures reveal that two of the three subunits, Tip20p and Dsl1p, resemble known subunits of the exocyst complex, establishing a structural connection among several multisubunit tethering complexes and implying that many of their subunits are derived from a common progenitor. We show, moreover, that Tip20p and Dsl1p interact directly via N-terminal alpha-helices. Finally, we establish that different Dsl1p complex subunits bind independently to different ER SNARE proteins. Our results map out two alternative protein-interaction networks capable of tethering COPI-coated vesicles, via the Dsl1p complex, to ER membranes.

Literature references that cite this PDB file's key reference

PubMed id

Reference

20643221

C.G.Angers, and A.J.Merz (2011).
New links between vesicle coats and Rab-mediated vesicle targeting.

Semin Cell Dev Biol, 22, 18-26.

21183348

J.S.Bonifacino, and A.Hierro (2011).
Transport according to GARP: receiving retrograde cargo at the trans-Golgi network.

Trends Cell Biol, 21, 159-167.

21235523

M.Hertzog, and P.Chavrier (2011).
Cell polarity during motile processes: keeping on track with the exocyst complex.

Biochem J, 433, 403-409.

20462487

A.Menant, and R.Karess (2010).
RZZ finds its ancestral roots.

Structure, 18, 549-550.

21056839

C.Bröcker, S.Engelbrecht-Vandré, and C.Ungermann (2010).
Multisubunit tethering complexes and their role in membrane fusion.

Curr Biol, 20, R943-R952.

21067454

F.C.Brown, and S.R.Pfeffer (2010).
An update on transport vesicle tethering.

Mol Membr Biol, 27, 457-461.

20462495

F.Civril, A.Wehenkel, F.M.Giorgi, S.Santaguida, A.Di Fonzo, G.Grigorean, F.D.Ciccarelli, and A.Musacchio (2010).
Structural analysis of the RZZ complex reveals common ancestry with multisubunit vesicle tethering machinery.

Structure, 18, 616-626.

PDB code:

3if8

20615984

F.J.Pérez-Victoria, G.Abascal-Palacios, I.Tascón, A.Kajava, J.G.Magadán, E.P.Pioro, J.S.Bonifacino, and A.Hierro (2010).
Structural basis for the wobbler mouse neurodegenerative disorder caused by mutation in the Vps54 subunit of the GARP complex.

Proc Natl Acad Sci U S A, 107, 12860-12865.

PDB codes:

3n1b 3n1e

19575650

I.M.Yu, and F.M.Hughson (2010).
Tethering factors as organizers of intracellular vesicular traffic.

Annu Rev Cell Dev Biol, 26, 137-156.

20972446

J.A.Lees, C.K.Yip, T.Walz, and F.M.Hughson (2010).
Molecular organization of the COG vesicle tethering complex.

Nat Struct Mol Biol, 17, 1292-1297.

20139078

K.Baek, A.Knödler, S.H.Lee, X.Zhang, K.Orlando, J.Zhang, T.J.Foskett, W.Guo, and R.Dominguez (2010).
Structure-function study of the N-terminal domain of exocyst subunit Sec3.

J Biol Chem, 285, 10424-10433.

PDB code:

3hie

21067450

M.Elias (2010).
Patterns and processes in the evolution of the eukaryotic endomembrane system.

Mol Membr Biol, 27, 469-489.

20065095

R.Fernández-Busnadiego, B.Zuber, U.E.Maurer, M.Cyrklaff, W.Baumeister, and V.Lucic (2010).
Quantitative analysis of the native presynaptic cytomatrix by cryoelectron tomography.

J Cell Biol, 188, 145-156.

19394211

A.Spang (2009).
On vesicle formation and tethering in the ER-Golgi shuttle.

Curr Opin Cell Biol, 21, 531-536.

19651599

B.C.Richardson, R.D.Smith, D.Ungar, A.Nakamura, P.D.Jeffrey, V.V.Lupashin, and F.M.Hughson (2009).
Structural basis for a human glycosylation disorder caused by mutation of the COG4 gene.

Proc Natl Acad Sci U S A, 106, 13329-13334.

PDB code:

3hr0

19887069

E.Sztul, and V.Lupashin (2009).
Role of vesicle tethering factors in the ER-Golgi membrane traffic.

FEBS Lett, 583, 3770-3783.

19346454

R.J.Perry, F.D.Mast, and R.A.Rachubinski (2009).
Endoplasmic reticulum-associated secretory proteins Sec20p, Sec39p, and Dsl1p are involved in peroxisome biogenesis.

Eukaryot Cell, 8, 830-843.

20005805

Y.Ren, C.K.Yip, A.Tripathi, D.Huie, P.D.Jeffrey, T.Walz, and F.M.Hughson (2009).
A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.

Cell, 139, 1119-1129.

PDB code:

3k8p

The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB code is shown on the right.