3AB3

Crystal structure of p115RhoGEF RGS domain in complex with G alpha 13


Experimental Data Snapshot

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.205 

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Ligand Structure Quality Assessment 


This is version 1.4 of the entry. See complete history


Literature

Identification of critical residues in G(alpha)13 for stimulation of p115RhoGEF activity and the structure of the G(alpha)13-p115RhoGEF regulator of G protein signaling homology (RH) domain complex.

Hajicek, N.Kukimoto-Niino, M.Mishima-Tsumagari, C.Chow, C.R.Shirouzu, M.Terada, T.Patel, M.Yokoyama, S.Kozasa, T.

(2011) J Biol Chem 286: 20625-20636

  • DOI: https://doi.org/10.1074/jbc.M110.201392
  • Primary Citation of Related Structures:  
    3AB3

  • PubMed Abstract: 

    RH-RhoGEFs are a family of guanine nucleotide exchange factors that contain a regulator of G protein signaling homology (RH) domain. The heterotrimeric G protein Gα(13) stimulates the guanine nucleotide exchange factor (GEF) activity of RH-RhoGEFs, leading to activation of RhoA. The mechanism by which Gα(13) stimulates the GEF activity of RH-RhoGEFs, such as p115RhoGEF, has not yet been fully elucidated. Here, specific residues in Gα(13) that mediate activation of p115RhoGEF are identified. Mutation of these residues significantly impairs binding of Gα(13) to p115RhoGEF as well as stimulation of GEF activity. These data suggest that the exchange activity of p115RhoGEF is stimulated allosterically by Gα(13) and not through its interaction with a secondary binding site. A crystal structure of Gα(13) bound to the RH domain of p115RhoGEF is also presented, which differs from a previously crystallized complex with a Gα(13)-Gα(i1) chimera. Taken together, these data provide new insight into the mechanism by which p115RhoGEF is activated by Gα(13).


  • Organizational Affiliation

    Department of Pharmacology, College of Medicine, University of Illinois, Chicago, Illinois 60612, USA.


Macromolecules
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Entity ID: 1
MoleculeChains Sequence LengthOrganismDetailsImage
Guanine nucleotide-binding protein G(k) subunit alpha, Guanine nucleotide-binding protein subunit alpha-13
A, C
362Mus musculusMutation(s): 0 
Gene Names: Gna13Gna-13
UniProt & NIH Common Fund Data Resources
Find proteins for P27601 (Mus musculus)
Explore P27601 
Go to UniProtKB:  P27601
IMPC:  MGI:95768
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupP27601
Sequence Annotations
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  • Reference Sequence
Find similar proteins by:  (by identity cutoff)  |  3D Structure
Entity ID: 2
MoleculeChains Sequence LengthOrganismDetailsImage
Rho guanine nucleotide exchange factor 1
B, D
246Homo sapiensMutation(s): 0 
Gene Names: ARHGEF1
UniProt & NIH Common Fund Data Resources
Find proteins for Q92888 (Homo sapiens)
Explore Q92888 
Go to UniProtKB:  Q92888
PHAROS:  Q92888
GTEx:  ENSG00000076928 
Entity Groups  
Sequence Clusters30% Identity50% Identity70% Identity90% Identity95% Identity100% Identity
UniProt GroupQ92888
Sequence Annotations
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  • Reference Sequence
Experimental Data & Validation

Experimental Data

  • Method: X-RAY DIFFRACTION
  • Resolution: 2.40 Å
  • R-Value Free: 0.280 
  • R-Value Work: 0.205 
  • R-Value Observed: 0.205 
  • Space Group: P 1
Unit Cell:
Length ( Å )Angle ( ˚ )
a = 50.481α = 77.77
b = 70.64β = 84.45
c = 88.078γ = 80.11
Software Package:
Software NamePurpose
MOLREPphasing
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: 2010-12-29
    Type: Initial release
  • Version 1.1: 2011-07-13
    Changes: Version format compliance
  • Version 1.2: 2013-10-30
    Changes: Database references
  • Version 1.3: 2017-08-23
    Changes: Refinement description, Source and taxonomy
  • Version 1.4: 2023-11-01
    Changes: Data collection, Database references, Derived calculations, Refinement description