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

0354275 - MBÚ 2011 RIV GB eng J - Journal Article
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-Structural Biology and Crystallization Communications. Roč. 66, - (2010), s. 1119-1123. ISSN 1744-3091. E-ISSN 2053-230X
R&D Projects: GA MŠMT(CZ) LC06010; GA ČR GP310/06/P150
Institutional research plan: CEZ:AV0Z50200510; CEZ:AV0Z50520514; CEZ:AV0Z60870520; CEZ:AV0Z40550506
Keywords : Fe-regulated protein D * iron-regulated proteins * outer membrane lipoproteins
Subject RIV: EC - Immunology
Impact factor: 0.563, year: 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
Permanent Link: http://hdl.handle.net/11104/0193316