[English] 日本語
Yorodumi Papers
- Database of articles cited by EMDB/PDB/SASBDB data -

+
Search query

Keywords
Structure methods
Author
Journal
IF

-
Structure paper

TitleStructural insights into coffee bitter taste perception by TAS2R43 receptor.
Journal, issue, pagesNat Struct Mol Biol, Vol. 33, Issue 4, Page 701-710, Year 2026
Publish dateApr 20, 2026
AuthorsYoojoong Kim / Ryan H Gumpper / Yuxuan Zhuang / Ron O Dror / Bryan L Roth /
PubMed AbstractBitter taste functions as a means of both protection against potentially toxic compounds and savoring bitter tasting foods and beverages. Among the 26 bitter taste receptors, taste receptor type 2 ...Bitter taste functions as a means of both protection against potentially toxic compounds and savoring bitter tasting foods and beverages. Among the 26 bitter taste receptors, taste receptor type 2 member 43 (TAS2R43) has been identified as key for recognizing the bitter taste of coffee. TAS2R43 has also been implicated in many other physiological processes, including the regulation of glucagon-like peptide 1 release from the intestine, bronchodilation, innate immunity and metabolism. Here we report cryo-electron microscopy structures of human TAS2R43 coupled with inhibitory G protein or gustducin (G) stabilized by the potent nephrotoxin and carcinogen aristolochic acid I. Both structures revealed that aristolochic acid I binds in a presumed orthosteric pocket shared with other bitter taste receptor. Further structural, functional and computational studies revealed potential modes for coffee's constituents including caffeine and cafestol, which are bitter tastants from coffee. Lastly, long-timescale molecular dynamics simulations identified potential cryptic allosteric pockets in TAS2R43. These structures could accelerate the search for specific bitter taste ligands that ultimately may be therapeutically useful.
External linksNat Struct Mol Biol / PubMed:42009777 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.2 Å
Structure data

EMDB-70964, PDB-9oxa:
CryoEM structure of Gi-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-70965, PDB-9oxb:
CryoEM structure of Ggust-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-71038: Consensus map for Gi-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-71040: Local map of GPCR region of Gi-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-71041: Local map of Gi region for Gi-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-71043: Consensus map of Ggust-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-71044: Local map of GPCR region of Ggust-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-71046: Local map of Ggust region of Ggust-coupled TAS2R43 with aristolochic acid I
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-GOQ:
8-methoxy-6-nitro-naphtho[1,2-e][1,3]benzodioxole-5-carboxylic acid

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
KeywordsSIGNALING PROTEIN / GPCR

+
About Yorodumi Papers

-
News

-
Feb 9, 2022. New format data for meta-information of EMDB entries

New format data for meta-information of EMDB entries

  • Version 3 of the EMDB header file is now the official format.
  • The previous official version 1.9 will be removed from the archive.

Related info.:EMDB header

External links:wwPDB to switch to version 3 of the EMDB data model

-
Aug 12, 2020. Covid-19 info

Covid-19 info

URL: https://pdbj.org/emnavi/covid19.php

New page: Covid-19 featured information page in EM Navigator.

Related info.:Covid-19 info / Mar 5, 2020. Novel coronavirus structure data

+
Mar 5, 2020. Novel coronavirus structure data

Novel coronavirus structure data

Related info.:Yorodumi Speices / Aug 12, 2020. Covid-19 info

External links:COVID-19 featured content - PDBj / Molecule of the Month (242):Coronavirus Proteases

+
Jan 31, 2019. EMDB accession codes are about to change! (news from PDBe EMDB page)

EMDB accession codes are about to change! (news from PDBe EMDB page)

  • The allocation of 4 digits for EMDB accession codes will soon come to an end. Whilst these codes will remain in use, new EMDB accession codes will include an additional digit and will expand incrementally as the available range of codes is exhausted. The current 4-digit format prefixed with “EMD-” (i.e. EMD-XXXX) will advance to a 5-digit format (i.e. EMD-XXXXX), and so on. It is currently estimated that the 4-digit codes will be depleted around Spring 2019, at which point the 5-digit format will come into force.
  • The EM Navigator/Yorodumi systems omit the EMD- prefix.

Related info.:Q: What is EMD? / ID/Accession-code notation in Yorodumi/EM Navigator

External links:EMDB Accession Codes are Changing Soon! / Contact to PDBj

+
Jul 12, 2017. Major update of PDB

Major update of PDB

  • wwPDB released updated PDB data conforming to the new PDBx/mmCIF dictionary.
  • This is a major update changing the version number from 4 to 5, and with Remediation, in which all the entries are updated.
  • In this update, many items about electron microscopy experimental information are reorganized (e.g. em_software).
  • Now, EM Navigator and Yorodumi are based on the updated data.

External links:wwPDB Remediation / Enriched Model Files Conforming to OneDep Data Standards Now Available in the PDB FTP Archive

-
Yorodumi Papers

Database of articles cited by EMDB/PDB/SASBDB data

  • Database of articles cited by EMDB, PDB, and SASBDB entries
  • Using PubMed data

Related info.:EMDB / PDB / SASBDB / Yorodumi / EMN Papers / Changes in new EM Navigator and Yorodumi

Read more