Premium
The crystal structure of the TCP domain of PCF6 in Oryza sativa L. reveals an RHH‐like fold
Author(s) -
Sun Lifang,
Zou Xiaoming,
Jiang Meiqin,
Wu Xiuling,
Chen Yayu,
Wang Qianchao,
Wang Qin,
Chen Lifei,
Wu Yunkun
Publication year - 2020
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13727
Subject(s) - helix (gastropod) , dna binding domain , biology , basic helix loop helix , repressor , structural similarity , protein structure , protein domain , transcription factor , genetics , microbiology and biotechnology , dna binding protein , biophysics , gene , biochemistry , ecology , snail
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.