PDBsum entry 4j2c

Protein transport

PDB id: 4j2c

Contents

Protein chains

108 a.a.

12 a.a.

Waters ×507

PDB id:

4j2c

Name:

Protein transport

Title:

Garp-snare interaction

Structure:

Syntaxin-6. Chain: a, c. Fragment: unp residues 3-110. Engineered: yes. Vacuolar protein sorting-associated protein 51 homolog. Chain: b, d. Fragment: unp residues 33-49. Synonym: another new gene 2 protein, protein fat-free homolog. Engineered: yes

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: stx6. Expressed in: escherichia coli. Expression_system_taxid: 562. Synthetic: yes. Organism_taxid: 9606

Resolution:

1.80Å R-factor: 0.155 R-free: 0.195

Authors:

G.Abascal-Palacios,C.Schindler,A.L.Rojas,J.S.Bonifacino,A.Hierro

Key ref:

G.Abascal-Palacios et al. (2013). Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6. Structure, 21, 1698-1706. PubMed id: 23932592 DOI: 10.1016/j.str.2013.06.025

Date:

04-Feb-13 Release date: 25-Dec-13

Protein chains

O43752  (STX6_HUMAN) -  Syntaxin-6 from Homo sapiens

Seq: 255 a.a.

Struc: 108 a.a.*

Protein chains

Q9UID3  (VPS51_HUMAN) -  Vacuolar protein sorting-associated protein 51 homolog from Homo sapiens

Seq: 782 a.a.

Struc: 12 a.a.

* PDB and UniProt seqs differ at 2 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chains A, B, C, D: E.C.?

DOI no: 10.1016/j.str.2013.06.025

Structure 21:1698-1706 (2013)

PubMed id: 23932592

Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.

G.Abascal-Palacios, C.Schindler, A.L.Rojas, J.S.Bonifacino, A.Hierro.

ABSTRACT

The Golgi-Associated Retrograde Protein (GARP) complex is a tethering factor involved in the fusion of endosome-derived transport vesicles to the trans-Golgi network through interaction with components of the Syntaxin 6/Syntaxin 16/Vti1a/VAMP4 SNARE complex. The mechanisms by which GARP and other tethering factors engage the SNARE fusion machinery are poorly understood. Herein, we report the structural basis for the interaction of the human Ang2 subunit of GARP with the Syntaxin 6 and the closely related Syntaxin 10. The crystal structure of the Syntaxin 6 Habc domain in complex with a peptide from the N terminus of Ang2 shows a binding mode in which a dityrosine motif of Ang2 interacts with a highly conserved groove in Syntaxin 6. Structure-based mutational analyses validate the crystal structure and support the phylogenetic conservation of this interaction.