5BV1

Crystal Structure of a Vps33-Vps16 Complex from Chaetomium thermophilum

Summary for 5BV1

• Entry DOI: 10.2210/pdb5bv1/pdb
• Related: 4KMO 5BUZ 5BV0
• Descriptor: VPS33, Putative vacuolar protein sorting-associated protein, D-MALATE (3 entities in total)
• Functional Keywords: membrane trafficking, sm protein, hops complex, thermophile, transport protein
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); More
• Total number of polymer chains: 4
• Total formula weight: 224072.83

Authors

Baker, R.W.,Jeffrey, P.D.,Hughson, F.M. (deposition date: 2015-06-04, release date: 2015-08-12, Last modification date: 2023-09-27)

Primary citation

Baker, R.W.,Jeffrey, P.D.,Zick, M.,Phillips, B.P.,Wickner, W.T.,Hughson, F.M.
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
Science, 349:1111-1114, 2015

PubMed Abstract: Fusion of intracellular transport vesicles requires soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) and Sec1/Munc18-family (SM) proteins. Membrane-bridging SNARE complexes are critical for fusion, but their spontaneous assembly is inefficient and may require SM proteins in vivo. We report x-ray structures of Vps33, the SM subunit of the yeast homotypic fusion and vacuole protein-sorting (HOPS) complex, bound to two individual SNAREs. The two SNAREs, one from each membrane, are held in the correct orientation and register for subsequent complex assembly. Vps33 and potentially other SM proteins could thus act as templates for generating partially zipped SNARE assembly intermediates. HOPS was essential to mediate SNARE complex assembly at physiological SNARE concentrations. Thus, Vps33 appears to catalyze SNARE complex assembly through specific SNARE motif recognition.

PubMed: 26339030
DOI: 10.1126/science.aac7906

Experimental method

X-RAY DIFFRACTION (2.902 Å)