PDBsum entry: 2pbi

Signaling protein

PDB-id: 2pbi

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Description

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Header records

References

PROCHECK

Protein chains

415 a.a. *

345 a.a. *

Ligands

GOL ×9

Waters ×890

* Residue conservation analysis

Tools

Clefts Calculation

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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)

Seq:
Struc:
	Seq:
	Struc:
Seq:		675 a.a.
Struc:		415 a.a.*

Chains B, D: P62881 (GBB5_MOUSE)

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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Surface

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.