3CUE

Crystal structure of a TRAPP subassembly activating the Rab Ypt1p


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.265 
  • R-Value Observed: 0.265 

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Literature

The structural basis for activation of the Rab Ypt1p by the TRAPP membrane-tethering complexes.

Cai, Y.Chin, H.F.Lazarova, D.Menon, S.Fu, C.Cai, H.Sclafani, A.Rodgers, D.W.De La Cruz, E.M.Ferro-Novick, S.Reinisch, K.M.

(2008) Cell 133: 1202-1213

  • DOI: https://doi.org/10.1016/j.cell.2008.04.049
  • Primary Citation of Related Structures:  
    3CUE

  • PubMed Abstract: 

    The multimeric membrane-tethering complexes TRAPPI and TRAPPII share seven subunits, of which four (Bet3p, Bet5p, Trs23p, and Trs31p) are minimally needed to activate the Rab GTPase Ypt1p in an event preceding membrane fusion. Here, we present the structure of a heteropentameric TRAPPI assembly complexed with Ypt1p. We propose that TRAPPI facilitates nucleotide exchange primarily by stabilizing the nucleotide-binding pocket of Ypt1p in an open, solvent-accessible form. Bet3p, Bet5p, and Trs23p interact directly with Ypt1p to stabilize this form, while the C terminus of Bet3p invades the pocket to participate in its remodeling. The Trs31p subunit does not interact directly with the GTPase but allosterically regulates the TRAPPI interface with Ypt1p. Our findings imply that TRAPPII activates Ypt1p by an identical mechanism. This view of a multimeric membrane-tethering assembly complexed with a Rab provides a framework for understanding events preceding membrane fusion at the molecular level.


  • Organizational Affiliation

    Department of Cell Biology, Yale University School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Transport protein particle 23 kDa subunit
A, G, M, S
219Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: TRS23
UniProt
Find proteins for Q03784 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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Go to UniProtKB:  Q03784
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UniProt GroupQ03784
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  • Reference Sequence
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Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Transport protein particle 31 kDa subunit
B, H, N, T
283Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: TRS31
UniProt
Find proteins for Q03337 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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UniProt GroupQ03337
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Entity ID: 3
MoleculeChains Sequence LengthOrganismDetailsImage
Transport protein particle 18 kDa subunit
C, I, O, U
159Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: BET5
UniProt
Find proteins for Q03630 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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UniProt GroupQ03630
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Entity ID: 4
MoleculeChains Sequence LengthOrganismDetailsImage
Transport protein particle 22 kDa subunit
D, E, J, K, P
D, E, J, K, P, Q, V, W
193Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: BET3
UniProt
Find proteins for P36149 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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  • Reference Sequence
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Entity ID: 5
MoleculeChains Sequence LengthOrganismDetailsImage
GTP-binding protein YPT1
F, L, R, X
206Saccharomyces cerevisiaeMutation(s): 0 
Gene Names: YPT1YP2
UniProt
Find proteins for P01123 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
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UniProt GroupP01123
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.70 Å
  • R-Value Free: 0.299 
  • R-Value Work: 0.265 
  • R-Value Observed: 0.265 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 115.12α = 90
b = 115.4β = 90.28
c = 290.07γ = 90
Software Package:
Software NamePurpose
ADSCdata collection
SHARPphasing
CNSrefinement
HKL-2000data reduction
HKL-2000data scaling

Structure Validation

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Ligand Structure Quality Assessment 


Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2008-07-08
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2012-03-21
    Changes: Database references