PDBsum entry 6fuf

Signaling protein

PDB id: 6fuf

Contents

Protein chains

316 a.a.

181 a.a.

Ligands

RET

NAG

Waters ×1

PDB id:

6fuf

Name:

Signaling protein

Title:

Crystal structure of the rhodopsin-mini-go complex

Structure:

Rhodopsin. Chain: a. Engineered: yes. Guanine nucleotide-binding protein g(o) subunit alpha. Chain: b. Engineered: yes

Source:

Bos taurus. Bovine. Organism_taxid: 9913. Gene: rho. Expressed in: homo sapiens. Expression_system_taxid: 9606. Expression_system_cell_line: hek293. Homo sapiens. Human.

Resolution:

3.12Å R-factor: 0.259 R-free: 0.280

Authors:

C.-J.Tsai,T.Weinert,J.Muehle,F.Pamula,R.Nehme,T.Flock,P.Nogly, P.C.Edwards,B.Carpenter,T.Gruhl,P.Ma,X.Deupi,J.Standfuss,C.G.Tate, G.F.X.Schertler

Key ref:

C.J.Tsai et al. (2018). Crystal structure of rhodopsin in complex with a mini-G_o sheds light on the principles of G protein selectivity. Sci Adv, 4, eaat7052. PubMed id: 30255144

Date:

27-Feb-18 Release date: 03-Oct-18

Protein chain

P02699  (OPSD_BOVIN) -  Rhodopsin from Bos taurus

Seq: 348 a.a.

Struc: 316 a.a.*

Protein chain

P09471  (GNAO_HUMAN) -  Guanine nucleotide-binding protein G(o) subunit alpha from Homo sapiens

Seq: 354 a.a.

Struc: 181 a.a.*

* PDB and UniProt seqs differ at 29 residue positions (black crosses)

Enzyme reactions

• Enzyme class: Chain B: E.C.3.6.5.- - ?????

Sci Adv 4:eaat7052 (2018)

PubMed id: 30255144

Crystal structure of rhodopsin in complex with a mini-G_o sheds light on the principles of G protein selectivity.

C.J.Tsai, F.Pamula, R.Nehmé, J.Mühle, T.Weinert, T.Flock, P.Nogly, P.C.Edwards, B.Carpenter, T.Gruhl, P.Ma, X.Deupi, J.Standfuss, C.G.Tate, G.F.X.Schertler.

ABSTRACT

Selective coupling of G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptors (GPCRs) to specific Gα-protein subtypes is critical to transform extracellular signals, carried by natural ligands and clinical drugs, into cellular responses. At the center of this transduction event lies the formation of a signaling complex between the receptor and G protein. We report the crystal structure of light-sensitive GPCR rhodopsin bound to an engineered mini-G_o protein. The conformation of the receptor is identical to all previous structures of active rhodopsin, including the complex with arrestin. Thus, rhodopsin seems to adopt predominantly one thermodynamically stable active conformation, effectively acting like a "structural switch," allowing for maximum efficiency in the visual system. Furthermore, our analysis of the well-defined GPCR-G protein interface suggests that the precise position of the carboxyl-terminal "hook-like" element of the G protein (its four last residues) relative to the TM7/helix 8 (H8) joint of the receptor is a significant determinant in selective G protein activation.