3ONJ

Crystal structure of yeast Vti1p_Habc domain

Summary for 3ONJ

• Entry DOI: 10.2210/pdb3onj/pdb
• Related: 3ONK 3ONL
• Descriptor: t-SNARE VTI1 (2 entities in total)
• Functional Keywords: helix, habc, protein transport
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Prevacuolar compartment membrane; Single- pass type IV membrane protein: Q04338
• Total number of polymer chains: 1
• Total formula weight: 10995.16

Authors

Wang, J.,Fang, P.,Niu, L.,Teng, M. (deposition date: 2010-08-29, release date: 2011-07-20, Last modification date: 2023-11-01)

Primary citation

Wang, J.,Gossing, M.,Fang, P.,Zimmermann, J.,Li, X.,von Mollard, G.F.,Niu, L.,Teng, M.
Epsin N-terminal homology domains bind on opposite sides of two SNAREs
Proc.Natl.Acad.Sci.USA, 108:12277-12282, 2011

PubMed Abstract: SNARE proteins are crucial for membrane fusion in vesicular transport. To ensure efficient and accurate fusion, SNAREs need to be sorted into different budding vesicles. This process is usually regulated by specific recognition between SNAREs and their adaptor proteins. How different pairs of SNAREs and adaptors achieve their recognition is unclear. Here, we report the recognition between yeast SNARE Vti1p and its adaptor Ent3p derived from three crystal structures. Surprisingly, this yeast pair Vti1p/Ent3p interacts through a distinct binding site compared to their homologues vti1b/epsinR in mammals. An opposite surface on Vti1p_Habc domain binds to a conserved area on the epsin N-terminal homology (ENTH) domain of Ent3p. Two-hybrid, in vitro pull-down and in vivo experiments indicate this binding interface is important for correct localization of Vti1p in the cell. This previously undescribed discovery that a cargo and adaptor pair uses different binding sites across species suggests the diversity of SNARE-adaptor recognition in vesicular transport.

PubMed: 21746902
DOI: 10.1073/pnas.1013101108

Experimental method

X-RAY DIFFRACTION (1.92 Å)