PDBsum entry 5olv

Membrane protein

PDB id: 5olv

Contents

Protein chain

388 a.a.

Ligands

9Y2

CLR ×4

OLA ×13

OLC ×10

Metals

_NA

Waters ×115

PDB id:

5olv

Name:

Membrane protein

Title:

Structure of the a2a-star2-bril562-luaa47070 complex at 2.0a obtained from in meso soaking experiments.

Structure:

Adenosine receptor a2a,soluble cytochrome b562,adenosine receptor a2a. Chain: a. Synonym: cytochrome b-562. Engineered: yes. Mutation: yes

Source:

Homo sapiens, escherichia coli. Human. Organism_taxid: 9606, 562. Gene: adora2a, adora2, cybc. Expressed in: trichoplusia ni. Expression_system_taxid: 7111.

Resolution:

2.00Å R-factor: 0.181 R-free: 0.208

Authors:

P.Rucktooa,R.K.Y.Cheng,E.Segala,T.Geng,J.C.Errey,G.A.Brown,R.Cooke, F.H.Marshall,A.S.Dore

Key ref:

P.Rucktooa et al. (2018). Towards high throughput GPCR crystallography: In Meso soaking of Adenosine A_2AReceptor crystals. Sci Rep, 8, 41. PubMed id: 29311713

Date:

28-Jul-17 Release date: 17-Jan-18

Protein chain

P0ABE7  (C562_ECOLX) -  Soluble cytochrome b562 from Escherichia coli

Seq: 128 a.a.

Struc: 388 a.a.*

Protein chain

P29274  (AA2AR_HUMAN) -  Adenosine receptor A2a from Homo sapiens

Seq: 412 a.a.

Struc: 388 a.a.*

* PDB and UniProt seqs differ at 119 residue positions (black crosses)

Sci Rep 8:41 (2018)

PubMed id: 29311713

Towards high throughput GPCR crystallography: In Meso soaking of Adenosine A_2AReceptor crystals.

P.Rucktooa, R.K.Y.Cheng, E.Segala, T.Geng, J.C.Errey, G.A.Brown, R.M.Cooke, F.H.Marshall, A.S.Doré.

ABSTRACT

Here we report an efficient method to generate multiple co-structures of the A_2AG protein-coupled receptor (GPCR) with small-molecules from a single preparation of a thermostabilised receptor crystallised in Lipidic Cubic Phase (LCP). Receptor crystallisation is achieved following purification using a low affinity "carrier" ligand (theophylline) and crystals are then soaked in solutions containing the desired (higher affinity) compounds. Complete datasets to high resolution can then be collected from single crystals and seven structures are reported here of which three are novel. The method significantly improves structural throughput for ligand screening using stabilised GPCRs, thereby actively driving Structure-Based Drug Discovery (SBDD).