1WID

Solution Structure of the B3 DNA-Binding Domain of RAV1

1WID の概要

• エントリーDOI: 10.2210/pdb1wid/pdb
• 分子名称: DNA-binding protein RAV1 (1 entity in total)
• 機能のキーワード: dna-binding domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, dna binding protein
• 由来する生物種: Arabidopsis thaliana (thale cress)
• 細胞内の位置: Nucleus (Probable): Q9ZWM9
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 14315.89

構造登録者

Yamasaki, K.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2004-05-28, 公開日: 2004-11-28, 最終更新日: 2024-05-29)

主引用文献

Yamasaki, K.,Kigawa, T.,Inoue, M.,Tateno, M.,Yamasaki, T.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Tomo, Y.,Hayami, N.,Terada, T.,Shirouzu, M.,Osanai, T.,Tanaka, A.,Seki, M.,Shinozaki, K.,Yokoyama, S.
Solution Structure of the B3 DNA Binding Domain of the Arabidopsis Cold-Responsive Transcription Factor RAV1
Plant Cell, 16:3448-3459, 2004

PubMed Abstract: The B3 DNA binding domain is shared amongst various plant-specific transcription factors, including factors involved in auxin-regulated and abscisic acid-regulated transcription. Herein, we report the NMR solution structure of the B3 domain of the Arabidopsis thaliana cold-responsive transcription factor RAV1. The structure consists of a seven-stranded open beta-barrel and two alpha-helices located at the ends of the barrel and is significantly similar to the structure of the noncatalytic DNA binding domain of the restriction enzyme EcoRII. An NMR titration experiment revealed a DNA recognition interface that enabled us to propose a structural model of the protein-DNA complex. The locations of the DNA-contacting residues are also likely to be similar to those of the EcoRII DNA binding domain.

PubMed: 15548737
DOI: 10.1105/tpc.104.026112

実験手法

SOLUTION NMR