6CMV

Crystal structure of Archaeal Biofilm Regulator (AbfR2) from Sulfolobus acidocaldarius

6CMV の概要

• エントリーDOI: 10.2210/pdb6cmv/pdb
• 分子名称: Transcriptional regulator Lrs14-like protein, GLYCEROL, (4S)-2-METHYL-2,4-PENTANEDIOL, ... (4 entities in total)
• 機能のキーワード: whth, archaea, biofilm, gene regulation
• 由来する生物種: Sulfolobus acidocaldarius
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 101163.63

構造登録者

Essen, L.-O.,Vogt, M.S.,Banerjee, A. (登録日: 2018-03-06, 公開日: 2018-11-14, 最終更新日: 2024-11-13)

主引用文献

Vogt, M.S.,Volpel, S.L.,Albers, S.V.,Essen, L.O.,Banerjee, A.
Crystal structure of an Lrs14-like archaeal biofilm regulator from Sulfolobus acidocaldarius.
Acta Crystallogr D Struct Biol, 74:1105-1114, 2018

PubMed Abstract: The small winged helix-turn-helix (wHTH) proteins of the Lrs14 family are major transcriptional regulators and act as archaeal biofilm regulators (AbfRs) in the crenarchaeote Sulfolobus acidocaldarius. Here, the first crystal structure of an AbfR ortholog, AbfR2, the deletion of which is known to impair biofilm formation, is presented. Like most other wHTH orthologs, AbfR2 is dimeric in solution as well as in its 2.45 Å resolution crystal structure. Given the presence of three independent AbfR2 dimers in the asymmetric unit, the crystal structure shows a considerable degree of conformational variation within the dimer, the antiparallel orientations of which are stabilized by coiled-coil interaction between H4 helices. Conserved anchor interactions between helices H0 and H4 of AbfR2 further contribute to dimer stabilization. The combined structural and bioinformatic analysis reveals cluster-specific structural differences between different members of the Lrs14 protein family.

PubMed: 30387769
DOI: 10.1107/S2059798318014146

実験手法

X-RAY DIFFRACTION (2.45 Å)