Intercalation of Trioxatriangulenium Ion in DNA:  Binding, Electron Transfer, X-ray Crystallography, and Electronic Structure

2003 ◽  
Vol 125 (8) ◽  
pp. 2072-2083 ◽  
Author(s):  
Jóhannes Reynisson ◽  
Gary B. Schuster ◽  
Sheldon B. Howerton ◽  
Loren Dean Williams ◽  
Robert N. Barnett ◽  
...  
Keyword(s):  
Electron Transfer ◽  
Electronic Structure ◽  
Dna Binding ◽  
X Ray ◽  
X Ray Crystallography

DNA binding by the plant-specific NAC transcription factors in crystal and solution: a firm link to WRKY and GCM transcription factors

2012 ◽  
Vol 444 (3) ◽  
pp. 395-404 ◽  
Author(s):  
Ditte H. Welner ◽  
Søren Lindemose ◽  
J. Günter Grossmann ◽  
Niels Erik Møllegaard ◽  
Addie N. Olsen ◽  
...  
Keyword(s):  
Transcription Factors ◽  
Dna Binding ◽  
Stress Responses ◽  
Crystal Form ◽  
Nutrient Distribution ◽  
Nac Domain ◽  
X Ray ◽  
Nac Transcription Factors ◽  
X Ray Crystallography ◽  
Dna Complex

NAC (NAM/ATAF/CUC) plant transcription factors regulate essential processes in development, stress responses and nutrient distribution in important crop and model plants (rice, Populus, Arabidopsis), which makes them highly relevant in the context of crop optimization and bioenergy production. The structure of the DNA-binding NAC domain of ANAC019 has previously been determined by X-ray crystallography, revealing a dimeric and predominantly β-fold structure, but the mode of binding to cognate DNA has remained elusive. In the present study, information from low resolution X-ray structures and small angle X-ray scattering on complexes with oligonucleotides, mutagenesis and (DNase I and uranyl photo-) footprinting, is combined to form a structural view of DNA-binding, and for the first time provide experimental evidence for the speculated relationship between plant-specific NAC proteins, WRKY transcription factors and the mammalian GCM (Glial cell missing) transcription factors, which all use a β-strand motif for DNA-binding. The structure shows that the NAC domain inserts the edge of its core β-sheet into the major groove, while leaving the DNA largely undistorted. The structure of the NAC–DNA complex and a new crystal form of the unbound NAC also indicate limited flexibility of the NAC dimer arrangement, which could be important in recognizing suboptimal binding sites.

scholarly journals Synthesis, characterization, X-ray crystallography and DNA binding activities of Co(III) and Cu(II) complexes with a pyrimidine-based Schiff base ligand

2016 ◽  
Vol 442 ◽  
pp. 70-80 ◽  
Author(s):  
Rajesh Pradhan ◽  
Milon Banik ◽  
David B. Cordes ◽  
Alexandra M.Z. Slawin ◽  
Nitis Chandra Saha
Keyword(s):  
Schiff Base ◽  
Dna Binding ◽  
Schiff Base Ligand ◽  
X Ray ◽  
X Ray Crystallography

Anticancer activity, DNA binding and docking study of M(II)-complexes (M=Zn, Cu and Ni) derived from a new pyrazine-thiazole ligand: Synthesis, structure and DFT

2021 ◽  
Author(s):  
Pradip Bera ◽  
Abhishek Aher ◽  
Paula Brandão ◽  
Sunil Manna ◽  
Indranil Bhattacharyya ◽  
...  
Keyword(s):  
Density Functional Theory ◽  
Dna Binding ◽  
Anticancer Activity ◽  
Density Functional ◽  
Docking Study ◽  
Functional Theory ◽  
X Ray ◽  
X Ray Crystallography ◽  
Ligand Synthesis

A series of structurally related Zn(II), Cu(II) and Ni(II) complexes of 4-(2-(2-(1-(pyrazin-2-yl)ethylidene)hydrazinyl)-thiazol-4-yl)-benzonitrile (PyztbH) have been synthesized and characterized by spectroscopy, single X-ray crystallography and density functional theory (DFT). All the...

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