3QOE

Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11

3QOE の概要

• エントリーDOI: 10.2210/pdb3qoe/pdb
• 関連するPDBエントリー: 3QOD
• 分子名称: Heterocyst differentiation protein (2 entities in total)
• 機能のキーワード: mcsg, psi biology, structural genomics, midwest center for structural genomics, helix-turn-helix, transcription factor, dna binding protein
• 由来する生物種: Fischerella thermalis
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 70467.09

構造登録者

Kim, Y.,Joachimiak, G.,Gornicki, P.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (登録日: 2011-02-09, 公開日: 2011-04-20, 最終更新日: 2023-09-13)

主引用文献

Kim, Y.,Joachimiak, G.,Ye, Z.,Binkowski, T.A.,Zhang, R.,Gornicki, P.,Callahan, S.M.,Hess, W.R.,Haselkorn, R.,Joachimiak, A.
Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.
Proc.Natl.Acad.Sci.USA, 108:10109-10114, 2011

PubMed Abstract: HetR is an essential regulator of heterocyst development in cyanobacteria. HetR binds to a DNA palindrome upstream of the hetP gene. We report the crystal structure of HetR from Fischerella at 3.0 Å. The protein is a dimer comprised of a central DNA-binding unit containing the N-terminal regions of the two subunits organized with two helix-turn-helix motifs; two globular flaps extending in opposite directions; and a hood over the central core formed from the C-terminal subdomains. The flaps and hood have no structural precedent in the protein database, therefore representing new folds. The structural assignments are supported by site-directed mutagenesis and DNA-binding studies. We suggest that HetR serves as a scaffold for assembly of transcription components critical for heterocyst development.

PubMed: 21628585
DOI: 10.1073/pnas.1106840108

実験手法

X-RAY DIFFRACTION (3.004 Å)