4yrv

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

spinqualitylabelsall models 4yrv, resolution 2.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4yrv is a 4 chain structure with sequence from Nostoc sp. PCC 7120 = FACHB-418. This structure supersedes the now removed PDB entry 4k1m. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.8Å Ligands: CA Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function HETR_NOSS1 Controls heterocyst differentiation. Has both a protease and a DNA-binding activity. Binds the promoter regions of hetR, hepA and patS. Publication Abstract from PubMed 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 A, respectively. The intertwined HetR dimer possesses a couple of novel HTH motifs, each of which consists of two canonical alpha-helices in the DNA-binding domain and an auxiliary alpha-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 alpha-helix and eventually release of HetR from the DNA major grove. These findings provide the structural insights into a prokaryotic example of Turing model. Structural insights into HetR-PatS interaction involved in cyanobacterial pattern formation.,Hu HX, Jiang YL, Zhao MX, Cai K, Liu S, Wen B, Lv P, Zhang Y, Peng J, Zhong H, Yu HM, Ren YM, Zhang Z, Tian C, Wu Q, Oliveberg M, Zhang CC, Chen Y, Zhou CZ Sci Rep. 2015 Nov 18;5:16470. doi: 10.1038/srep16470. PMID:26576507 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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