PDBsum entry 4pxf

Signaling protein

PDB id: 4pxf

Contents

Protein chain

325 a.a.

Ligands

ASP-ILE-ASP-VAL-MET-GLY-LEU

NAG-NAG-BMA-MAN

GLC-GLC

BOG ×3

PLM

SO4

ACT

Waters ×12

PDB id:

4pxf

Name:

Signaling protein

Title:

Crystal structure of the active g-protein-coupled receptor opsin in complex with the finger-loop peptide derived from the full-length arrestin-1

Structure:

Rhodopsin. Chain: a. S-arrestin. Chain: b. Engineered: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Other_details: bovine eye. Synthetic: yes. Bovine,cow,domestic cattle,domestic cow. Organism_taxid: 9913

Resolution:

2.75Å R-factor: 0.217 R-free: 0.251

Authors:

M.Szczepek,P.Scheerer

Key ref:

M.Szczepek et al. (2014). Crystal structure of a common GPCR-binding interface for G protein and arrestin. Nat Commun, 5, 4801. PubMed id: 25205354 DOI: 10.1038/ncomms5801

Date:

23-Mar-14 Release date: 17-Sep-14

Protein chain

P02699  (OPSD_BOVIN) -  Rhodopsin from Bos taurus

Seq: 348 a.a.

Struc: 325 a.a.

DOI no: 10.1038/ncomms5801

Nat Commun 5:4801 (2014)

PubMed id: 25205354

Crystal structure of a common GPCR-binding interface for G protein and arrestin.

M.Szczepek, F.Beyrière, K.P.Hofmann, M.Elgeti, R.Kazmin, A.Rose, F.J.Bartl, D.von Stetten, M.Heck, M.E.Sommer, P.W.Hildebrand, P.Scheerer.

ABSTRACT

G-protein-coupled receptors (GPCRs) transmit extracellular signals to activate intracellular heterotrimeric G proteins (Gαβγ) and arrestins. For G protein signalling, the Gα C-terminus (GαCT) binds to a cytoplasmic crevice of the receptor that opens upon activation. A consensus motif is shared among GαCT from the Gi/Gt family and the 'finger loop' region (ArrFL1-4) of all four arrestins. Here we present a 2.75 Å crystal structure of ArrFL-1, a peptide analogue of the finger loop of rod photoreceptor arrestin, in complex with the prototypical GPCR rhodopsin. Functional binding of ArrFL to the receptor was confirmed by ultraviolet-visible absorption spectroscopy, competitive binding assays and Fourier transform infrared spectroscopy. For both GαCT and ArrFL, binding to the receptor crevice induces a similar reverse turn structure, although significant structural differences are seen at the rim of the binding crevice. Our results reflect both the common receptor-binding interface and the divergent biological functions of G proteins and arrestins.