Další formáty:
BibTeX
LaTeX
RIS
@article{549940, author = {Šnajdrová, Lenka and Kulhánek, Petr and Imberty, Anne and Koča, Jaroslav}, article_number = {5}, keywords = {Galactosyltransferase; Molecular dynamics; Loops opening; Structural water molecules}, language = {eng}, issn = {0008-6215}, journal = {Carbohydrate Research}, title = {Molecular dynamics simulations of glycosyltransferase LgtC}, url = {http://www.sciencedirect.com/science/article/B6TFF-4BJX0MM-1/2/40cffae104186599da947477ce5752b7}, volume = {339}, year = {2004} }
TY - JOUR ID - 549940 AU - Šnajdrová, Lenka - Kulhánek, Petr - Imberty, Anne - Koča, Jaroslav PY - 2004 TI - Molecular dynamics simulations of glycosyltransferase LgtC JF - Carbohydrate Research VL - 339 IS - 5 SP - 995-1006 EP - 995-1006 SN - 00086215 KW - Galactosyltransferase KW - Molecular dynamics KW - Loops opening KW - Structural water molecules UR - http://www.sciencedirect.com/science/article/B6TFF-4BJX0MM-1/2/40cffae104186599da947477ce5752b7 N2 - Molecular dynamics simulations have been performed on fully solvated alpha-(1->4)-galactosyltransferase LgtC from Neisseria meningitidis with and without the donor substrate UDP-Gal and in the presence of the manganese ion. The analysis of the trajectories revealed a limited movement in the loop X (residues 75-80) and a larger conformational change in the loop Y (residues 246-251) in the simulation, when UDP-Gal was not present. In this case, the loops X and Y open by almost 10 A, exposing the active site to the solvent. The 'hinge region' responsible for the opening is composed of residues 246-247. We have also analyzed the behavior of the manganese ion in the simulations. The coordination number is 6 when UDP-Gal is present and it increases to 7 when it is absent. In the latter case, three water molecules become coordinated to the ion. In both cases, the coordination is very stable implying that the manganese ion is tightly bound in the active site of the enzyme even if UDP-Gal is not present. Further analysis of the structural water molecules location confirmed that the mobility of water molecules in the active site and the accessibility of this site for solvent are higher in the absence of the substrate. ER -
ŠNAJDROVÁ, Lenka, Petr KULHÁNEK, Anne IMBERTY a Jaroslav KOČA. Molecular dynamics simulations of glycosyltransferase LgtC. \textit{Carbohydrate Research}. 2004, roč.~339, č.~5, s.~995-1006. ISSN~0008-6215.
|