4YNL

Crystal structure of the hood domain of Anabaena HetR in complex with the hexapeptide ERGSGR derived from PatS

Summary for 4YNL

• Entry DOI: 10.2210/pdb4ynl/pdb
• Related: 4YRV
• Descriptor: Heterocyst differentiation control protein, Heterocyst inhibition-signaling peptide (3 entities in total)
• Functional Keywords: heterocyst differentiation, transcription factor, transcription
• Biological source: Nostoc sp. PCC 7120; More
• Cellular location: Periplasm : O52748
• Total number of polymer chains: 8
• Total formula weight: 46640.81

Authors

Hu, H.X.,Jiang, Y.L.,Zhao, M.X.,Zhang, C.C.,Chen, Y.,Zhou, C.Z. (deposition date: 2015-03-10, release date: 2015-12-02, Last modification date: 2023-11-08)

Primary citation

Hu, H.X.,Jiang, Y.L.,Zhao, M.X.,Cai, K.,Liu, S.,Wen, B.,Lv, P.,Zhang, Y.,Peng, J.,Zhong, H.,Yu, H.M.,Ren, Y.M.,Zhang, Z.,Tian, C.,Wu, Q.,Oliveberg, M.,Zhang, C.C.,Chen, Y.,Zhou, C.Z.
Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation
Sci Rep, 5:16470-16470, 2015

PubMed Abstract: The one-dimensional pattern of heterocyst in the model cyanobacterium Anabaena sp. PCC 7120 is coordinated by the transcription factor HetR and PatS peptide. Here we report the complex structures of HetR binding to DNA, and its hood domain (HetRHood) binding to a PatS-derived hexapeptide (PatS6) at 2.80 and 2.10 Å, respectively. The intertwined HetR dimer possesses a couple of novel HTH motifs, each of which consists of two canonical α-helices in the DNA-binding domain and an auxiliary α-helix from the flap domain of the neighboring subunit. Two PatS6 peptides bind to the lateral clefts of HetRHood, and trigger significant conformational changes of the flap domain, resulting in dissociation of the auxiliary α-helix and eventually release of HetR from the DNA major grove. These findings provide the structural insights into a prokaryotic example of Turing model.

PubMed: 26576507
DOI: 10.1038/srep16470

Experimental method

X-RAY DIFFRACTION (2.1 Å)