4J01

Crystal Structure of Fischerella Transcription Factor HetR complexed with 29mer DNA target

Summary for 4J01

• Entry DOI: 10.2210/pdb4j01/pdb
• Related: 4IZZ 4J00
• Descriptor: Transcription Factor HetR, DNA (29-MER), SULFATE ION, ... (4 entities in total)
• Functional Keywords: structural genomics, psi-biology, midwest center for structural genomics, mcsg, helix-turn-helix, dna-binding domain, transcription factor, transcription-dna complex, transcription/dna
• Biological source: Fischerella thermalis; More
• Total number of polymer chains: 8
• Total formula weight: 176685.04

Authors

Kim, Y.,Joachimiak, G.,Gornicki, P.,Joachimiak, A.,MCSG,Midwest Center for Structural Genomics (MCSG) (deposition date: 2013-01-30, release date: 2013-03-27, Last modification date: 2023-09-20)

Primary citation

Kim, Y.,Ye, Z.,Joachimiak, G.,Videau, P.,Young, J.,Hurd, K.,Callahan, S.M.,Gornicki, P.,Zhao, J.,Haselkorn, R.,Joachimiak, A.
Structures of complexes comprised of Fischerella transcription factor HetR with Anabaena DNA targets.
Proc.Natl.Acad.Sci.USA, 110:E1716-E1723, 2013

PubMed Abstract: HetR is an essential regulator of heterocyst development in cyanobacteria. Many mutations in HetR render Anabaena incapable of nitrogen fixation. The protein binds to a DNA palindrome upstream of hetP and other genes. We have determined the crystal structures of HetR complexed with palindromic DNA targets, 21, 23, and 29 bp at 2.50-, 3.00-, and 3.25-Å resolution, respectively. The highest-resolution structure shows fine details of specific protein-DNA interactions. The lower-resolution structures with longer DNA duplexes have similar interaction patterns and show how the flap domains interact with DNA in a sequence nonspecific fashion. Fifteen of 15 protein-DNA contacts predicted on the basis of the structure were confirmed by single amino acid mutations that abolished binding in vitro and complementation in vivo. A striking feature of the structure is the association of glutamate 71 from each subunit of the HetR dimer with three successive cytosines in each arm of the palindromic target, a feature that is conserved among all known heterocyst-forming cyanobacteria sequenced to date.

PubMed: 23610410
DOI: 10.1073/pnas.1305971110

Experimental method

X-RAY DIFFRACTION (3.246 Å)