3QOD

Crystal Structure of Heterocyst Differentiation Protein, HetR from Fischerella mv11

Summary for 3QOD

• Entry DOI: 10.2210/pdb3qod/pdb
• Related: 3QOE
• Descriptor: Heterocyst differentiation protein (2 entities in total)
• Functional Keywords: structural genomics, psi-biology, midwest center for structural genomics, mcsg, helix-turn-helix, transcription factor, cytosol, dna binding protein
• Biological source: Fischerella thermalis
• Total number of polymer chains: 2
• Total formula weight: 71967.73

Authors

Kim, Y.,Joachimiak, G.,Gornicki, P.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2011-02-09, release date: 2011-04-20, Last modification date: 2024-10-30)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.38 Å)