5YZY

AtVAL1 B3 domain in complex with 13bp-DNA

Summary for 5YZY

• Entry DOI: 10.2210/pdb5yzy/pdb
• Descriptor: DNA (5'-D(*AP*TP*TP*CP*TP*GP*CP*AP*TP*GP*GP*AP*T)-3'), DNA (5'-D(*TP*AP*TP*CP*CP*AP*TP*GP*CP*AP*GP*AP*A)-3'), B3 domain-containing transcription repressor VAL1, ... (4 entities in total)
• Functional Keywords: transcriptional factor, val1, b3 domain, dna complex, flc, plant, transcription-dna complex, transcription/dna
• Biological source: Arabidopsis thaliana (Mouse-ear cress); More
• Cellular location: Nucleus : Q8W4L5
• Total number of polymer chains: 3
• Total formula weight: 22336.03

Authors

Wu, B.X.,Zhang, M.M. (deposition date: 2017-12-17, release date: 2018-05-02, Last modification date: 2024-03-27)

Primary citation

Wu, B.X.,Zhang, M.M.,Su, S.C.,Liu, H.H.,Gan, J.H.,Ma, J.B.
Structural insight into the role of VAL1 B3 domain for targeting to FLC locus in Arabidopsis thaliana.
Biochem. Biophys. Res. Commun., 2018

PubMed Abstract: Vernalization is a pivotal stage for some plants involving many epigenetic changes during cold exposure. In Arabidopsis, an essential step in vernalization for further flowering is successful silence the potent floral repressor Flowering Locus C (FLC) by repressing histone mark. AtVal1 is a multi-function protein containing five domains that participate into many recognition processes and is validated to recruit the repress histone modifier PHD-PRC2 complex and interact with components of the ASAP complex target to the FLC nucleation region through recognizing a cis element known as CME (cold memory element) by its plant-specific B3 domain. Here, we determine the crystal structure of the B3 domain in complex with Sph/RY motif in CME. Our structural analysis reveals the specific DNA recognition by B3 domain, combined with our in vitro experiments, we provide the structural insight into the important implication of AtVAL1-B3 domain in flowering process.

PubMed: 29733847
DOI: 10.1016/j.bbrc.2018.05.002

Experimental method

X-RAY DIFFRACTION (2.61 Å)