1VYH

PAF-AH Holoenzyme: Lis1/Alfa2


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.264 
  • R-Value Observed: 0.265 

wwPDB Validation   3D Report Full Report


This is version 1.3 of the entry. See complete history


Literature

Coupling Paf Signaling to Dynein Regulation: Structure of Lis1 in Complex with Paf-Acetylhydrolase.

Tarricone, C.Perrina, F.Monzani, S.Massimiliano, L.Kim, M.H.Derewenda, Z.S.Knapp, S.Tsai, L.-H.Musacchio, A.

(2004) Neuron 44: 809

  • DOI: https://doi.org/10.1016/j.neuron.2004.11.019
  • Primary Citation of Related Structures:  
    1VYH

  • PubMed Abstract: 

    Mutations in the LIS1 gene cause lissencephaly, a human neuronal migration disorder. LIS1 binds dynein and the dynein-associated proteins Nde1 (formerly known as NudE), Ndel1 (formerly known as NUDEL), and CLIP-170, as well as the catalytic alpha dimers of brain cytosolic platelet activating factor acetylhydrolase (PAF-AH). The mechanism coupling the two diverse regulatory pathways remains unknown. We report the structure of LIS1 in complex with the alpha2/alpha2 PAF-AH homodimer. One LIS1 homodimer binds symmetrically to one alpha2/alpha2 homodimer via the highly conserved top faces of the LIS1 beta propellers. The same surface of LIS1 contains sites of mutations causing lissencephaly and overlaps with a putative dynein binding surface. Ndel1 competes with the alpha2/alpha2 homodimer for LIS1, but the interaction is complex and requires both the N- and C-terminal domains of LIS1. Our data suggest that the LIS1 molecule undergoes major conformational rearrangement when switching from a complex with the acetylhydrolase to the one with Ndel1.


  • Organizational Affiliation

    Department of Experimental Oncology, European Institute of Oncology, Via Ripamonti 435, 20141 Milan, Italy.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB BETA SUBUNIT
A, B, E, F, I
A, B, E, F, I, J, M, N, Q, R
229Homo sapiensMutation(s): 0 
EC: 3.1.1.47
UniProt & NIH Common Fund Data Resources
Find proteins for P68402 (Homo sapiens)
Explore P68402 
Go to UniProtKB:  P68402
PHAROS:  P68402
GTEx:  ENSG00000168092 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP68402
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
PLATELET-ACTIVATING FACTOR ACETYLHYDROLASE IB ALPHA SUBUNIT
C, D, G, H, K
C, D, G, H, K, L, O, P, S, T
410Mus musculusMutation(s): 0 
UniProt
Find proteins for P63005 (Mus musculus)
Explore P63005 
Go to UniProtKB:  P63005
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP63005
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.40 Å
  • R-Value Free: 0.307 
  • R-Value Work: 0.264 
  • R-Value Observed: 0.265 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 205.77α = 90
b = 101.22β = 98.06
c = 246.13γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
AMoREphasing

Structure Validation

View Full Validation Report



Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2005-05-26
    Type: Initial release
  • Version 1.1: 2011-05-08
    Changes: Version format compliance
  • Version 1.2: 2011-07-13
    Changes: Version format compliance
  • Version 1.3: 2023-12-13
    Changes: Data collection, Database references, Other, Refinement description