Počet záznamů: 1

Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis

  1. 1.
    0354275 - MBU-M 2011 RIV GB eng J - Článek v odborném periodiku
    Sviridova, E. - Bumba, Ladislav - Řezáčová, Pavlína - Procházková, Kateřina - Kavan, Daniel - Bezouška, Karel - Kutý, Michal - Šebo, Peter - Kutá-Smatanová, Ivana
    Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis.
    Acta Crystallographica Section F. Roč. 66, - (2010), s. 1119-1123 ISSN 1744-3091
    Grant CEP: GA MŠk(CZ) LC06010; GA ČR GP310/06/P150
    Výzkumný záměr: CEZ:AV0Z50200510; CEZ:AV0Z50520514; CEZ:AV0Z60870520; CEZ:AV0Z40550506
    Klíčová slova: Fe-regulated protein D * iron-regulated proteins * outer membrane lipoproteins
    Kód oboru RIV: EC - Imunologie
    Impakt faktor: 0.563, rok: 2010

    Fe-regulated protein D (FrpD) is a Neisseria meningitidis outer membrane lipoprotein that may be involved in the anchoring of the secreted repeat in toxins (RTX) protein FrpC to the outer bacterial membrane. However, the function and biological roles of the FrpD and FrpC proteins remain unknown. Native and selenomethionine-subsituted variants of recombinant FrpD43-271 protein were crystalized using the sitting-drop vapour-diffusion method. Diffraction data were collected to a resolution of 2.25 Å for native FrpD43-271 protein and to a resolution of 2.00 Å for selenomethionine-subsitute FrpD43-271 (SeMet FrpD43-271 ) protein. The crystals of native FrdP43-271 protein belonged to the hexagonal space group P62 or P64, while the crystals of SeMet FrpD43-271 protein belonged to the primitive orthorhombic space group P212121
    Trvalý link: http://hdl.handle.net/11104/0193316