7FDN

Crystal structure of transcription factor WER in complex with EGL3

Summary for 7FDN

• Entry DOI: 10.2210/pdb7fdn/pdb
• Descriptor: Transcription factor EGL1, SULFATE ION, GLYCEROL, ... (6 entities in total)
• Functional Keywords: transcription factor, transcription
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 43874.37

Authors

Luo, Q.,Wang, B. (deposition date: 2021-07-17, release date: 2022-07-20, Last modification date: 2023-11-29)

Primary citation

Wang, B.,Luo, Q.,Li, Y.,Du, K.,Wu, Z.,Li, T.,Shen, W.H.,Huang, C.H.,Gan, J.,Dong, A.
Structural insights into partner selection for MYB and bHLH transcription factor complexes.
Nat.Plants, 8:1108-1117, 2021

PubMed Abstract: MYB and basic helix-loop-helix (bHLH) transcription factors form complexes to regulate diverse metabolic and developmental processes in plants. However, the molecular mechanisms responsible for MYB-bHLH interaction and partner selection remain unclear. Here, we report the crystal structures of three MYB-bHLH complexes (WER-EGL3, CPC-EGL3 and MYB29-MYC3), uncovering two MYB-bHLH interaction modes. WER and CPC are R2R3- and R3-type MYBs, respectively, but interact with EGL3 through their N-terminal R3 domain in a similar mode. A single amino acid of CPC, Met49, is crucial for competition with WER to interact with EGL3. MYB29, a R2R3-type MYB transcription factor, interacts with MYC3 by its C-terminal MYC-interaction motif. The WER-EGL3 and MYB29-MYC3 binding modes are widely applied among MYB-bHLH complexes in Arabidopsis and evolve independently in plants.

PubMed: 35995835
DOI: 10.1038/s41477-022-01223-w

Experimental method

X-RAY DIFFRACTION (1.9 Å)