3K8P

Structural basis for vesicle tethering by the Dsl1 complex

Summary for 3K8P

• Entry DOI: 10.2210/pdb3k8p/pdb
• Descriptor: Dsl1, Protein transport protein SEC39 (3 entities in total)
• Functional Keywords: intracellular trafficking, dsl1 complex, multisubunit tethering complex, snare proteins, endoplasmic reticulum, er-golgi transport, membrane, protein transport, transport, transport protein-transport protein complex, transport protein/transport protein
• Biological source: Kluyveromyces lactis (Yeast); More
• Cellular location: Endoplasmic reticulum membrane; Peripheral membrane protein: Q12745
• Total number of polymer chains: 2
• Total formula weight: 125621.13

Authors

Ren, Y.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2009-10-14, release date: 2009-11-10, Last modification date: 2024-10-30)

Primary citation

Ren, Y.,Yip, C.K.,Tripathi, A.,Huie, D.,Jeffrey, P.D.,Walz, T.,Hughson, F.M.
A structure-based mechanism for vesicle capture by the multisubunit tethering complex Dsl1.
Cell(Cambridge,Mass.), 139:1119-1129, 2009

PubMed Abstract: Vesicle trafficking requires membrane fusion, mediated by SNARE proteins, and upstream events that probably include "tethering," an initial long-range attachment between a vesicle and its target organelle. Among the factors proposed to mediate tethering are a set of multisubunit tethering complexes (MTCs). The Dsl1 complex, with only three subunits, is the simplest known MTC and is essential for the retrograde traffic of COPI-coated vesicles from the Golgi to the ER. To elucidate structural principles underlying MTC function, we have determined the structure of the Dsl1 complex, revealing a tower containing at its base the binding sites for two ER SNAREs and at its tip a flexible lasso for capturing vesicles. The Dsl1 complex binds to individual SNAREs via their N-terminal regulatory domains and also to assembled SNARE complexes; moreover, it is capable of accelerating SNARE complex assembly. Our results suggest that even the simplest MTC may be capable of orchestrating vesicle capture, uncoating, and fusion.

PubMed: 20005805
DOI: 10.1016/j.cell.2009.11.002

Experimental method

X-RAY DIFFRACTION (2.6 Å)