1WID

Solution Structure of the B3 DNA-Binding Domain of RAV1

Summary for 1WID

• Entry DOI: 10.2210/pdb1wid/pdb
• Descriptor: DNA-binding protein RAV1 (1 entity in total)
• Functional Keywords: dna-binding domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, dna binding protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Nucleus (Probable): Q9ZWM9
• Total number of polymer chains: 1
• Total formula weight: 14315.89

Authors

Yamasaki, K.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-28, release date: 2004-11-28, Last modification date: 2024-05-29)

Primary citation

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

Experimental method

SOLUTION NMR