4Z8Y

Crystal structure of Rab GTPase Sec4p mutant - S29V

Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.239 

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Literature

New insights into the molecular mechanism of the Rab GTPase Sec4p activation.

Rinaldi, F.C., Packer, M., Collins, R.

(2015) BMC Struct Biol 15: 14-14

  • DOI: https://doi.org/10.1186/s12900-015-0041-5
  • Primary Citation of Related Structures:  
    4Z8Y, 4ZDW

  • PubMed Abstract: 

    Sec4p is a small monomeric Ras-related GTP-binding protein (23 kDa) that regulates polarized exocytosis in S. cerevisiae. In this study we examine the structural effects of a conserved serine residue in the P-loop corresponding to G12 in Ras.

    • Organizational Affiliation: 

    Department of Molecular Medicine, Cornell University, Ithaca, NY, 14853, USA. fcr23@cornell.edu.


Macromolecules
Find similar proteins by: 
(by identity cutoff)  |  3D Structure
Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Ras-related protein SEC4
A, B
170Saccharomyces cerevisiae S288CMutation(s): 1 
Gene Names: SEC4, SRO6, YFL005W
UniProt
Find proteins for P07560 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c))
Explore P07560 
Go to UniProtKB:  P07560
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP07560
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 1.90 Å
  • R-Value Free: 0.298 
  • R-Value Work: 0.236 
  • R-Value Observed: 0.239 
  • Space Group: P 1 21 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 31.72α = 90
b = 75.45β = 91.58
c = 66.23γ = 90
Software Package:
Software NamePurpose
REFMACrefinement
MOSFLMdata reduction
SCALAdata scaling
PHASERphasing

Structure Validation

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Entry History 

Deposition Data

Revision History  (Full details and data files)

  • Version 1.0: 2015-10-14
    Type: Initial release
  • Version 1.1: 2023-09-27
    Changes: Data collection, Database references, Derived calculations, Refinement description