4B27

Trp RNA-binding attenuation protein: modifying symmetry and stability of a circular oligomer

4B27 の概要

• エントリーDOI: 10.2210/pdb4b27/pdb
• 関連するPDBエントリー: 1WAP 3ZZQ
• 分子名称: TRANSCRIPTION ATTENUATION PROTEIN MTRB, TRYPTOPHAN (3 entities in total)
• 機能のキーワード: transcription, transcription regulation, thermofluor, protein engineering
• 由来する生物種: BACILLUS SUBTILIS
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 51448.38

構造登録者

Bayfield, O.W.,Chen, C.,Patterson, A.R.,Luan, W.,Smits, C.,Gollnick, P.,Antson, A.A. (登録日: 2012-07-12, 公開日: 2012-09-19, 最終更新日: 2023-12-20)

主引用文献

Bayfield, O.W.,Chen, C.,Patterson, A.R.,Luan, W.,Smits, C.,Gollnick, P.,Antson, A.A.
Trp RNA-Binding Attenuation Protein: Modifying Symmetry and Stability of a Circular Oligomer.
Plos One, 7:44309-, 2012

PubMed Abstract: Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for investigating determinants of the oligomeric state. A short segment of C-terminal residues defines whether TRAP forms an 11-mer or 12-mer assembly. To understand which oligomeric state is more stable, we examine the stability of several wild type and mutant TRAP proteins.

PubMed: 22970197
DOI: 10.1371/JOURNAL.PONE.0044309

実験手法

X-RAY DIFFRACTION (2.72 Å)