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5ZKT

Crystal structure of TCP domain of PCF6 in Oryza sativa

Summary for 5ZKT
Entry DOI10.2210/pdb5zkt/pdb
DescriptorPutative transcription factor PCF6 (2 entities in total)
Functional Keywordstcp domain, ospcf6, transcription
Biological sourceOryza sativa subsp. japonica (Rice)
Total number of polymer chains2
Total formula weight12436.34
Authors
Sun, L.F.,Zou, X.M.,Wu, Y.K. (deposition date: 2018-03-26, release date: 2019-03-27, Last modification date: 2026-02-11)
Primary citationSun, L.,Zou, X.,Jiang, M.,Wu, X.,Chen, Y.,Wang, Q.,Wang, Q.,Chen, L.,Wu, Y.
The crystal structure of the TCP domain of PCF6 in Oryza sativa L. reveals an RHH-like fold.
Febs Lett., 594:1296-1306, 2020
Cited by
PubMed Abstract: The Teosinte branched 1/Cycloidea/Proliferating cell factor (TCP) domain is an evolutionarily conserved DNA binding domain unique to the plant kingdom. To date, the functions of TCPs have been well studied, but the three-dimensional structure of the TCP domain is lacking. Here, we have determined the crystal structure of the TCP domain from OsPCF6. The structure reveals that the TCP domain adopts three short β-strands followed by a helix-loop-helix structure, distinct from the canonical basic helix-loop-helix structure. This folded domain shows high structural similarity to the ribbon-helix-helix (RHH) transcriptional repressors, a family of DNA binding proteins with a conserved 3D structural motif (RHH fold), indicating that TCPs could be reclassified as RHH proteins. Our work will provide insight toward a better understanding of the mechanisms underlying TCP protein function.
PubMed: 31898812
DOI: 10.1002/1873-3468.13727
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.74 Å)
Structure validation

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