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Signaling protein PDB id
2pbi
Jmol
Contents
Protein chains
415 a.a. *
345 a.a. *
Ligands
GOL ×9
Waters ×890
* Residue conservation analysis
PDB id:
2pbi
Name: Signaling protein
Title: The multifunctional nature of gbeta5/rgs9 revealed from its structure
Structure: Regulator of g-protein signaling 9. Chain: a, c. Fragment: residues 1-422. Engineered: yes. Guanine nucleotide-binding protein subunit beta 5 chain: b, d. Fragment: residues 43-395. Synonym: transducin beta chain 5, gbeta5. Engineered: yes
Source: Mus musculus. House mouse. Organism_taxid: 10090. Strain: c57bl/6j. Gene: rgs9. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: gnb5.
Resolution:
1.95Å     R-factor:   0.185     R-free:   0.225
Authors: M.L.Cheever,J.T.Snyder,S.Gershburg,D.P.Siderovski,T.K.Harden
Key ref:
M.L.Cheever et al. (2008). Crystal structure of the multifunctional Gbeta5-RGS9 complex. Nat Struct Biol, 15, 155-162. PubMed id: 18204463 DOI: 10.1038/nsmb.1377
Date:
28-Mar-07     Release date:   29-Jan-08    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chains
Pfam   ArchSchema ?
O54828  (RGS9_MOUSE) -  Regulator of G-protein signaling 9
Seq:
Struc: 		 
Seq:
Struc: 		675 a.a.
415 a.a.
Protein chains
Pfam   ArchSchema ?
P62881  (GBB5_MOUSE) -  Guanine nucleotide-binding protein subunit beta-5
Seq:
Struc: 		395 a.a.
345 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     heterotrimeric G-protein complex   1 term 
  Biological process     intracellular signal transduction   3 terms 
  Biochemical function     signal transducer activity     2 terms  

 

 
DOI no: 10.1038/nsmb.1377 Nat Struct Biol 15:155-162 (2008)
PubMed id: 18204463  
 
 
Crystal structure of the multifunctional Gbeta5-RGS9 complex.
M.L.Cheever, J.T.Snyder, S.Gershburg, D.P.Siderovski, T.K.Harden, J.Sondek.
 
  ABSTRACT  
 
Regulators of G-protein signaling (RGS) proteins enhance the intrinsic GTPase activity of G protein alpha (Galpha) subunits and are vital for proper signaling kinetics downstream of G protein-coupled receptors (GPCRs). R7 subfamily RGS proteins specifically and obligately dimerize with the atypical G protein beta5 (Gbeta5) subunit through an internal G protein gamma (Ggamma)-subunit-like (GGL) domain. Here we present the 1.95-A crystal structure of the Gbeta5-RGS9 complex, which is essential for normal visual and neuronal signal transduction. This structure reveals a canonical RGS domain that is functionally integrated within a molecular complex that is poised for integration of multiple steps during G-protein activation and deactivation.
 
  Selected figure(s)  
 
Figure 5.
(a) Ribbon diagram of the RGS9-RGS domain (green) interface with the G -subunit–like (GGL) domain (red) and G 5 (blue). G 5 loop residues contacting the RGS domain are purple. Bundle and terminal RGS subdomains are indicated with green lines. (b) Transparent ribbon diagram of the RGS domain (green) and G 5 (blue) with interfacial contact residues depicted as balls and sticks. (c) Superimposed structures from the isolated RGS9-RGS domain (wheat) and RGS9-RGS domains in complexes with G t/i (coral) and G 5 (green) are depicted as transparent ribbon diagrams along with the G 5 (blue) structure. 		Figure 6.
(a) A model of the membrane-relative orientation and interprotein interactions of the G 5–RGS9 complex. G 5 and RGS9, colored as in Figure 1, with G t/i (ref. 30; gold) docked and colored as in Figure 5d. A modeled N-terminal helix for G t/i is depicted as a cylinder, and a wheat-colored R9AP cartoon is positioned near the RGS9-Dishevelled/Egl-10/Pleckstrin homology (DEP) and RGS9-DEP helical extension (DHEX) domains.
 
  The above figures are reprinted from an Open Access publication published by Macmillan Publishers Ltd: Nat Struct Biol (2008, 15, 155-162) copyright 2008.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
19797210 F.S.Chen, H.Shim, D.Morhardt, R.Dallman, E.Krahn, L.McWhinney, A.Rao, S.J.Gold, and C.K.Chen (2010).
Functional redundancy of R7 RGS proteins in ON-bipolar cell dendrites.
  Invest Ophthalmol Vis Sci, 51, 686-693.  
19797214 J.Zhang, B.G.Jeffrey, C.W.Morgans, N.S.Burke, T.L.Haley, R.M.Duvoisin, and R.L.Brown (2010).
RGS7 and -11 complexes accelerate the ON-bipolar cell light response.
  Invest Ophthalmol Vis Sci, 51, 1121-1129.  
20453851 K.Xie, K.L.Allen, S.Kourrich, J.Colón-Saez, M.J.Thomas, K.Wickman, and K.A.Martemyanov (2010).
Gbeta5 recruits R7 RGS proteins to GIRK channels to regulate the timing of neuronal inhibitory signaling.
  Nat Neurosci, 13, 661-663.  
19923320 M.Y.Porter, and M.R.Koelle (2010).
RSBP-1 is a membrane-targeting subunit required by the Galpha(q)-specific but not the Galpha(o)-specific R7 regulator of G protein signaling in Caenorhabditis elegans.
  Mol Biol Cell, 21, 232-243.  
19376773 A.C.Howlett, A.J.Gray, J.M.Hunter, and B.M.Willardson (2009).
Role of Molecular Chaperones in G Protein {beta}5/Regulator of G Protein Signaling Dimer Assembly and G Protein {beta}{gamma} Dimer Specificity.
  J Biol Chem, 284, 16386-16399.  
19646992 E.J.Friedman, B.R.Temple, S.N.Hicks, J.Sondek, C.D.Jones, and A.M.Jones (2009).
Prediction of protein-protein interfaces on G-protein beta subunits reveals a novel phospholipase C beta2 binding domain.
  J Mol Biol, 392, 1044-1054.  
19521673 G.R.Anderson, E.Posokhova, and K.A.Martemyanov (2009).
The R7 RGS protein family: multi-subunit regulators of neuronal G protein signaling.
  Cell Biochem Biophys, 54, 33-46.  
19332565 G.R.Anderson, R.Lujan, and K.A.Martemyanov (2009).
Changes in striatal signaling induce remodeling of RGS complexes containing Gbeta5 and R7BP subunits.
  Mol Cell Biol, 29, 3033-3044.  
19042037 M.Jayaraman, H.Zhou, L.Jia, M.D.Cain, and K.J.Blumer (2009).
R9AP and R7BP: traffic cops for the RGS7 family in phototransduction and neuronal GPCR signaling.
  Trends Pharmacol Sci, 30, 17-24.  
19806206 R.Prasobh, and N.Manoj (2009).
The repertoire of heterotrimeric G proteins and RGS proteins in Ciona intestinalis.
  PLoS One, 4, e7349.  
19182865 S.L.Sandiford, and V.Z.Slepak (2009).
The Gbeta5-RGS7 complex selectively inhibits muscarinic M3 receptor signaling via the interaction between the third intracellular loop of the receptor and the DEP domain of RGS7.
  Biochemistry, 48, 2282-2289.  
19212142 W.E.McIntire (2009).
Structural determinants involved in the formation and activation of G protein betagamma dimers.
  Neurosignals, 17, 82-99.  
18488142 A.V.Smrcka (2008).
G protein betagamma subunits: central mediators of G protein-coupled receptor signaling.
  Cell Mol Life Sci, 65, 2191-2214.  
18611381 C.A.Johnston, A.J.Kimple, P.M.Giguère, and D.P.Siderovski (2008).
Structure of the parathyroid hormone receptor C terminus bound to the G-protein dimer Gbeta1gamma2.
  Structure, 16, 1086-1094.
PDB codes: 2qns 3kj5
18456304 T.G.Wensel (2008).
Signal transducing membrane complexes of photoreceptor outer segments.
  Vision Res, 48, 2052-2061.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.