Abstract

Three-dimensional models of FtsZ-protein complexes with GDP from Arabidopsis thaliana L. localized in cytosol (Entrez database code NP190843) and in chloroplasts (Entrez database code AAA82068) were developed. Crystal structure of the FtsZ-GDP complex from archaea Methanococcus jannaschii (PDB-code 1FSZ) was used as a matrix. Secondary structures of computed models contain ten beta-strands. A chloroplast form of FtsZ-protein has ten alpha-helices and four 3(10)-helices, whereas cytosolic form of protein has nine and three structures correspondently and neither a0-helix before nucleotide-binding domain nor C-terminal 3(10)-helix in secondary domain. The T2-loop of nucleotide-binding pocket of chloroplast form of FtsZ-ptotein in position 111 contains non-charged alanin residue instead of the charged one which is typical for cytosolic and bacterial forms of proteins. At low sequence homology of FtsZ-proteins (approximately 47%) the developed models demonstrate high coincidence with matrix both in the structures of nucleotide-binding pocket and in the whole molecule. The models are completely suitable for further studies of possible sites of binding with dinitroaniline herbicides.