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TitleCryo-EM structure of the cytosolic AhR complex.
Journal, issue, pagesStructure, Vol. 31, Issue 3, Page 295-308.e4, Year 2023
Publish dateMar 2, 2023
AuthorsZuoling Wen / Yuebin Zhang / Beirong Zhang / Yumo Hang / Li Xu / Yangsheng Chen / Qunhui Xie / Qun Zhao / Lihua Zhang / Guohui Li / Bin Zhao / Fei Sun / Yujia Zhai / Yun Zhu /
PubMed AbstractAryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures ...Aryl hydrocarbon receptor (AhR) is an important ligand-activated transcription factor involved in the regulation of various important physiological functions. Here, we report the cryo-EM structures of the Hsp90-AhR-p23 complex with or without bound XAP2, where the structure of the mouse AhR PAS-B domain is resolved. A highly conserved bridge motif of AhR is responsible for the interaction with the Hsp90 dimeric lumen. The ligand-free AhR PAS-B domain is attached to the Hsp90 dimer and is stabilized in the complex with bound XAP2. In addition, the DE-loop and a group of conserved pocket inner residues in the AhR PAS-B domain are found to be important for ligand binding. These results reveal the structural basis of the biological functions of AhR. Moreover, the protein purification method presented here allows the isolation of stable mouse AhR protein, which could be used to develop high-sensitivity biosensors for environmental pollutant detection.
External linksStructure / PubMed:36649707
MethodsEM (single particle)
Resolution3.2 - 3.5 Å
Structure data

33537

7y04

EMDB-33537, PDB-7y04:
Hsp90-AhR-p23 complex
Method: EM (single particle) / Resolution: 3.5 Å

34519

8h77

EMDB-34519, PDB-8h77:
Hsp90-AhR-p23-XAP2 complex
Method: EM (single particle) / Resolution: 3.2 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-BEF:
BERYLLIUM TRIFLUORIDE ION

Source
  • mus musculus (house mouse)
KeywordsCYTOSOLIC PROTEIN / Hsp90 / AhR / complex / p23 / PASB doamin / XAP2

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