5H5P

Crystal structure of Myelin-gene Regulatory Factor DNA binding domain

5H5P の概要

• エントリーDOI: 10.2210/pdb5h5p/pdb
• 分子名称: Myelin regulatory factor (2 entities in total)
• 機能のキーワード: ig fold transcription factor, er membrane protein, trimeric transcription factor, transcription
• 由来する生物種: Mus musculus (Mouse)
• 細胞内の位置: Myelin regulatory factor: Endoplasmic reticulum membrane ; Single-pass membrane protein. Myelin regulatory factor, N-terminal: Nucleus . Myelin regulatory factor, C-terminal: Endoplasmic reticulum membrane ; Single-pass membrane protein : Q3UR85
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21495.94

構造登録者

Shi, N.,Zhen, X.,Li, B. (登録日: 2016-11-09, 公開日: 2017-06-28, 最終更新日: 2024-10-30)

主引用文献

Zhen, X.,Li, B.,Hu, F.,Yan, S.,Meloni, G.,Li, H.,Shi, N.
Crystal structure of the DNA-binding domain of Myelin-gene Regulatory Factor.
Sci Rep, 7:3696-3696, 2017

PubMed Abstract: Myelin-gene Regulatory Factor (MyRF) is one of the master transcription factors controlling myelin formation and development in oligodendrocytes which is crucial for the powerful brain functions. The N-terminal of MyRF, which contains a proline-rich region and a DNA binding domain (DBD), is auto-cleaved from the ER membrane, and then enters the nucleus to participate in transcription regulation of the myelin genes. Here we report the crystal structure of MyRF DBD. It shows an Ig-fold like architecture which consists of two antiparallel β-sheets with 7 main strands, packing against each other, forming a β-sandwich. Compared to its homolog, Ndt80, MyRF has a smaller and less complex DBD lacking the helices and the big loops outside the core. Structural alignment reveals that MyRF DBD possess less interaction sites with DNA than Ndt80 and may bind only at the major groove of DNA. Moreover, the structure reveals a trimeric assembly, agreeing with the previous report that MyRF DBD functions as a trimer. The mutant that we designed based on the structure disturbed trimer formation, but didn't affect the auto-cleavage reaction. It demonstrates that the activation of self-cleavage reaction of MyRF is independent of the presence of its N-terminal DBD homotrimer. The structure reported here will help to understand the molecular mechanism underlying the important roles of MyRF in myelin formation and development.

PubMed: 28623291
DOI: 10.1038/s41598-017-03768-9

実験手法

X-RAY DIFFRACTION (2.461 Å)