4AFI

Complex between Vamp7 longin domain and fragment of delta-adaptin from AP3

Summary for 4AFI

• Entry DOI: 10.2210/pdb4afi/pdb
• Related: 2VX8
• Descriptor: AP-3 COMPLEX SUBUNIT DELTA-1, VESICLE-ASSOCIATED MEMBRANE PROTEIN 7, PRASEODYMIUM ION (3 entities in total)
• Functional Keywords: endocytosis, exocytosis, clathrin adaptor, chimera, fusion protein
• Biological source: HOMO SAPIENS (HUMAN); More
• Cellular location: Cytoplasmic vesicle, secretory vesicle membrane; Single-pass type IV membrane protein: P70280
• Total number of polymer chains: 2
• Total formula weight: 39394.30

Authors

Kent, H.M.,Evans, P.R.,Luzio, J.P.,Peden, A.A.,Owen, D.J. (deposition date: 2012-01-19, release date: 2012-05-30, Last modification date: 2023-12-20)

Primary citation

Kent, H.M.,Evans, P.R.,Schaefer, I.B.,Gray, S.R.,Sanderson, C.M.,Luzio, J.P.,Peden, A.A.,Owen, D.J.
Structural Basis of the Intracellular Sorting of the Snare Vamp7 by the Ap3 Adaptor Complex
Dev.Cell, 22:979-, 2012

PubMed Abstract: VAMP7 is involved in the fusion of late endocytic compartments with other membranes. One possible mechanism of VAMP7 delivery to these late compartments is via the AP3 trafficking adaptor. We show that the linker of the δ-adaptin subunit of AP3 binds the VAMP7 longin domain and determines the structure of their complex. Mutation of residues on both partners abolishes the interaction in vitro and in vivo. The binding of VAMP7 to δ-adaptin requires the VAMP7 SNARE motif to be engaged in SNARE complex formation and hence AP3 must transport VAMP7 when VAMP7 is part of a cis-SNARE complex. The absence of δ-adaptin causes destabilization of the AP3 complex in mouse mocha fibroblasts and mislocalization of VAMP7. The mislocalization can be rescued by transfection with wild-type δ-adaptin but not by δ-adaptin containing mutations that abolish VAMP7 binding, despite in all cases intact AP3 being present and LAMP1 trafficking being rescued.

PubMed: 22521722
DOI: 10.1016/J.DEVCEL.2012.01.018

Experimental method

X-RAY DIFFRACTION (2.8 Å)