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5IN1

Crystal Structure of the MRG701 chromodomain

Summary for 5IN1
Entry DOI10.2210/pdb5in1/pdb
Related4PLI
DescriptorMRG701, SULFATE ION, 1,2-ETHANEDIOL, ... (4 entities in total)
Functional Keywordsmrg701, chromodomain, transcription
Biological sourceOryza sativa (Rice)
Total number of polymer chains2
Total formula weight17847.67
Authors
Huang, Y.,Liu, Y. (deposition date: 2016-03-07, release date: 2017-03-01, Last modification date: 2023-11-08)
Primary citationLiu, Y.,Wu, H.,Yu, Y.,Huang, Y.
Structural studies on MRG701 chromodomain reveal a novel dimerization interface of MRG proteins in green plants
Protein Cell, 7:792-803, 2016
Cited by
PubMed Abstract: MRG proteins are conserved during evolution in fungi, flies, mammals and plants, and they can exhibit diversified functions. The animal MRGs were found to form various complexes to activate gene expression. Plant MRG1/2 and MRG702 were reported to be involved in the regulation of flowering time via binding to H3K36me3-marked flowering genes. Herein, we determined the crystal structure of MRG701 chromodomain (MRG701). MRG701 forms a novel dimerization fold both in crystal and in solution. Moreover, we found that the dimerization of MRG chromodomains is conserved in green plants. Our findings may provide new insights into the mechanism of MRGs in regulation of gene expression in green plants.
PubMed: 27638467
DOI: 10.1007/s13238-016-0310-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.4 Å)
Structure validation

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