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Signaling protein PDB-id
2pbi
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Protein chains
415 a.a. *
345 a.a. *
Ligands
GOL ×9
Waters ×890

* Residue conservation analysis
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PDB id: 2pbi
Name: Signaling protein
Title: The multifunctional nature of gbeta5/rgs9 revealed from its crystal 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.

Source:
Mus musculus. House mouse. Organism_taxid: 10090. Strain: c57bl/6j. Gene: rgs9. Expressed in: trichoplusia ni. Expression_system_taxid: 7111. Gene: gnb5.

UniProt:
Chains A, C: O54828 (RGS9_MOUSE)
Pfam   ArchSchema ?
Seq:
Struc:
Seq:
Struc:
Seq: 675 a.a.
Struc: 415 a.a.*

Chains B, D: P62881 (GBB5_MOUSE)
Pfam   ArchSchema ?
Seq:
Struc:
Seq: 395 a.a.
Struc: 345 a.a.
Key:    PfamA domain  PfamB domain
 Secondary structure  CATH domain
* PDB and UniProt seqs differ at 2 residue positions (black crosses)

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,J.Sondek

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
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    Key reference    
 
 
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 the author.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
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.  
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.  
19806206 R.Prasobh, and N.Manoj (2009).
The repertoire of heterotrimeric G proteins and RGS proteins in Ciona intestinalis.
  PLoS One, 4, e7349.  
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.