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PDBsum entry 5buz
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Transport protein
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PDB id
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5buz
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Contents |
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605 a.a.
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324 a.a.
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38 a.a.
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40 a.a.
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PDB id:
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| Name: |
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Transport protein
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Title:
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Crystal structure of a complex between the snare vam3 and the hops vps33-vps16 subcomplex from chaetomium thermophilum
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Structure:
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Sm (sec1/munc18-like) protein. Chain: a, d. Synonym: vps33. Engineered: yes. Putative vacuolar protein sorting-associated protein. Chain: b, e. Synonym: vps16. Engineered: yes. Snap receptor-like protein.
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Source:
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Chaetomium thermophilum (strain dsm 1495 / cbs 144.50 / imi 039719). Organism_taxid: 759272. Strain: dsm 1495 / cbs 144.50 / imi 039719. Gene: ctht_0057760. Expressed in: escherichia coli. Expression_system_taxid: 469008. Chaetomium thermophilum. Gene: ctht_0026760.
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Resolution:
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3.10Å
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R-factor:
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0.196
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R-free:
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0.233
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Authors:
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R.W.Baker,P.D.Jeffrey,F.M.Hughson
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Key ref:
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R.W.Baker
et al.
(2015).
A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
Science,
349,
1111-1114.
PubMed id:
DOI:
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Date:
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04-Jun-15
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Release date:
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05-Aug-15
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PROCHECK
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Headers
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References
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G0SCM5
(G0SCM5_CHATD) -
Small conjugating protein ligase-like protein from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq: Struc:
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806 a.a.
605 a.a.
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G0S6M7
(G0S6M7_CHATD) -
Probable vacuolar protein sorting-associated protein 16 homolog from Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Seq: Struc:
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816 a.a.
324 a.a.*
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Enzyme class:
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Chains A, B, C, D, E, F:
E.C.?
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DOI no:
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Science
349:1111-1114
(2015)
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PubMed id:
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A direct role for the Sec1/Munc18-family protein Vps33 as a template for SNARE assembly.
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R.W.Baker,
P.D.Jeffrey,
M.Zick,
B.P.Phillips,
W.T.Wickner,
F.M.Hughson.
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ABSTRACT
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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.
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');
}
}
| | |