4LNZ

Crystal structure of human Myosin 5b globular domain


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.11 Å
  • R-Value Free: 0.312 
  • R-Value Work: 0.253 

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This is version 1.2 of the entry. See complete history


Literature

Structural insights into the globular tails of the human type v myosins myo5a, myo5b, and myo5c.

Velvarska, H.Niessing, D.

(2013) PLoS One 8: e82065-e82065

  • DOI: https://doi.org/10.1371/journal.pone.0082065
  • Primary Citation of Related Structures:  
    4LLI, 4LNZ

  • PubMed Abstract: 

    Vertebrate type V myosins (MyoV) Myo5a, Myo5b, and Myo5c mediate transport of several different cargoes. All MyoV paralogs bind to cargo complexes mainly by their C-terminal globular domains. In absence of cargo, the globular domain of Myo5a inhibits its motor domain. Here, we report low-resolution SAXS models for the globular domains from human Myo5a, Myo5b, and Myo5c, which suggest very similar overall shapes of all three paralogs. We determined the crystal structures of globular domains from Myo5a and Myo5b, and provide a homology model for human Myo5c. When we docked the Myo5a crystal structure into a previously published electron microscopy density of the autoinhibited full-length Myo5a, only one domain orientation resulted in a good fit. This structural arrangement suggests the participation of additional region of the globular domain in autoinhibition. Quantification of the interaction of the Myo5a globular domain with its motor complex revealed a tight binding with dissociation half-life in the order of minutes, suggesting a rather slow transition between the active and inactive states.


  • Organizational Affiliation

    Institute of Structural Biology; Helmholtz Zentrum München - German Research Center for Environmental Health, Neuherberg, Germany ; Gene Center and Department of Biochemistry, Ludwig-Maximilians-University, München, Germany.


Macromolecules
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Unconventional myosin-Vb394Homo sapiensMutation(s): 0 
Gene Names: MYO5BKIAA1119
UniProt & NIH Common Fund Data Resources
Find proteins for Q9ULV0 (Homo sapiens)
Explore Q9ULV0 
Go to UniProtKB:  Q9ULV0
PHAROS:  Q9ULV0
GTEx:  ENSG00000167306 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ9ULV0
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 3.11 Å
  • R-Value Free: 0.312 
  • R-Value Work: 0.253 
  • Space Group: P 21 21 2
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 60.644α = 90
b = 78.442β = 90
c = 86.606γ = 90
Software Package:
Software NamePurpose
PHENIXrefinement
PDB_EXTRACTdata extraction
ADSCdata collection
XDSdata reduction
SCALAdata scaling
SHARPphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2013-12-25
    Type: Initial release
  • Version 1.1: 2014-01-15
    Changes: Database references
  • Version 1.2: 2024-02-28
    Changes: Data collection, Database references