title: Interdomain compactization in human tyrosyl-tRNA synthetase studied by the hierarchical rotations technique.
abstract: Aminoacyl-tRNA synthetases are key enzymes of protein biosynthesis which usually possess multidomain structures. Mammalian tyrosyl-tRNA synthetase is composed of two structural modules: N-terminal catalytic core and an EMAPII-like C-terminal domain separated by long flexible linker. The structure of full-length human cytoplasmic tyrosyl-tRNA synthetase is still unknown. The structures of isolated N-terminal and C-terminal domains of the protein are resolved, but their compact packing in a functional enzyme is a subject of debates. In this work we studied putative compactization of the N- and C-terminal modules of human tyrosyl-tRNA synthetase by the coarse-grained hierarchical rotations technique (HIEROT). The large number of distinct types of binding interfaces between N- and C-terminal modules is revealed in the absence of enzyme substrates. The binding propensities of different residues are computed and several binding "hot spots" are observed on the surfaces of N and C modules. These results could be used to govern atomistic molecular dynamics simulations, which will sample preferable binding interfaces effectively.
authors.affiliation: Department of Physics of Biological Systems, Institute of Physics, National Academy of Sciences of Ukraine, Kiev, Ukraine. yesint3@yahoo.com
authors.forename: S O
authors.initials: SO
authors.lastname: Yesylevskyy
authors.forename: O V
authors.initials: OV
authors.lastname: Savytskyi
authors.forename: K A
authors.initials: KA
authors.lastname: Odynets
authors.forename: A I
authors.initials: AI
authors.lastname: Kornelyuk
mesh_terms: D006801:Humans; D017434:Protein Structure, Tertiary; D012399:Rotation; D013816:Thermodynamics; D014448:Tyrosine-tRNA Ligase / Q000737:chemistry*
chemical_list: D014448:Tyrosine-tRNA Ligase