Structural highlights
Publication Abstract from PubMed
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 A. 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.
Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria.,Kim Y, Joachimiak G, Ye Z, Binkowski TA, Zhang R, Gornicki P, Callahan SM, Hess WR, Haselkorn R, Joachimiak A Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10109-14. Epub 2011 May 31. PMID:21628585[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kim Y, Joachimiak G, Ye Z, Binkowski TA, Zhang R, Gornicki P, Callahan SM, Hess WR, Haselkorn R, Joachimiak A. Structure of transcription factor HetR required for heterocyst differentiation in cyanobacteria. Proc Natl Acad Sci U S A. 2011 Jun 21;108(25):10109-14. Epub 2011 May 31. PMID:21628585 doi:10.1073/pnas.1106840108
