4J2C

GARP-SNARE Interaction

Summary for 4J2C

• Entry DOI: 10.2210/pdb4j2c/pdb
• Descriptor: Syntaxin-6, Vacuolar protein sorting-associated protein 51 homolog (3 entities in total)
• Functional Keywords: tethering complex, protein transport
• Biological source: Homo sapiens (human); More
• Cellular location: Golgi apparatus membrane ; Single-pass type IV membrane protein : O43752; Golgi apparatus, trans-Golgi network : Q9UID3
• Total number of polymer chains: 4
• Total formula weight: 28982.24

Authors

Abascal-Palacios, G.,Schindler, C.,Rojas, A.L.,Bonifacino, J.S.,Hierro, A. (deposition date: 2013-02-04, release date: 2013-12-25, Last modification date: 2024-02-28)

Primary citation

Abascal-Palacios, G.,Schindler, C.,Rojas, A.L.,Bonifacino, J.S.,Hierro, A.
Structural basis for the interaction of the Golgi-Associated Retrograde Protein Complex with the t-SNARE Syntaxin 6.
Structure, 21:1698-1706, 2013

PubMed 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.

PubMed: 23932592
DOI: 10.1016/j.str.2013.06.025

Experimental method

X-RAY DIFFRACTION (1.801 Å)