3VUQ

Crystal structure of TTHA0167, a transcriptional regulator, TetR/AcrR family from Thermus thermophilus HB8

3VUQ の概要

• エントリーDOI: 10.2210/pdb3vuq/pdb
• 分子名称: Transcriptional regulator (TetR/AcrR family) (2 entities in total)
• 機能のキーワード: helix-turn-helix, transcriptional regulator, dna binding, transcription regulator
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 85487.63

構造登録者

Agari, Y.,Sakamoto, K.,Agari, K.,Kuramitsu, S.,Shinkai, A. (登録日: 2012-07-04, 公開日: 2013-02-27, 最終更新日: 2024-11-20)

主引用文献

Agari, Y.,Sakamoto, K.,Yutani, K.,Kuramitsu, S.,Shinkai, A.
Structure and function of a TetR family transcriptional regulator, SbtR, from thermus thermophilus HB8
Proteins, 81:1166-1178, 2013

PubMed Abstract: SbtR is one of the four TetR family transcriptional regulators present in the extremely thermophilic bacterium, Thermus thermophilus HB8. We identified 10 genes controlled by four promoters with negative regulation by SbtR in vitro. The SbtR-regulated gene products include probable transporters, probable enzymes for sugar or amino acid metabolism, and nucleic acid-related enzymes. SbtR binds pseudopalindromic sequences, with the consensus sequence of 5'-TGACCCNNKGGTCA-3' surrounding the promoters, and has a proposed 1:1 dimer binding stoichiometry. The X-ray crystal structure analysis revealed that SbtR comprises either nine or 10 α-helices and forms a dimer, as in the typical TetR family proteins. Similar to many characterized TetR family regulators, SbtR has a predicted ligand-binding pocket at the center of each monomer. Interestingly, the SbtR dimer contains an intermolecular disulfide bridge, formed between the Cys164 residues at the entrance of the pocket. The Cys164Ser and Cys164Ala mutant SbtR proteins formed homodimers similar to that of the wild type, but their thermal stabilities were lower by about 8°C, indicating that the disulfide bridge contributes to the thermal stability of the protein. However, altered repression activity of the mutants was not observed in vitro. From these results, we propose that ligand-binding is essential for SbtR to disengage from DNA, in a similar manner to the other characterized TetR family regulators. The formation and reduction of the disulfide bond might function in controlling the ligand-binding affinity of this transcriptional regulator.

PubMed: 23408580
DOI: 10.1002/prot.24266

実験手法

X-RAY DIFFRACTION (2.05 Å)