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4YRV

Crystal structure of Anabaena transcription factor HetR complexed with 21-bp DNA from hetP promoter

Replaces:  4K1M
Summary for 4YRV
Entry DOI10.2210/pdb4yrv/pdb
Related3QOD 4HRI
DescriptorHeterocyst differentiation control protein, DNA (5'-D(P*GP*CP*GP*AP*GP*GP*GP*GP*TP*CP*TP*AP*AP*CP*CP*CP*CP*TP*CP*AP*T)-3'), DNA (5'-D(P*AP*TP*GP*AP*GP*GP*GP*GP*TP*TP*AP*GP*AP*CP*CP*CP*CP*TP*CP*GP*C)-3'), ... (5 entities in total)
Functional Keywordsheterocyst differentiation, transcription factor, complex, transcription-dna complex, transcription/dna
Biological sourceNostoc sp. PCC 7120
More
Total number of polymer chains4
Total formula weight85117.52
Authors
Hu, H.X.,Jiang, Y.L.,Zhao, M.X.,Zhang, C.C.,Chen, Y.,Zhou, C.Z. (deposition date: 2015-03-16, release date: 2015-12-02, Last modification date: 2023-11-08)
Primary citationHu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.8 Å)
Structure validation

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