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

SYSNO ASEP	0354275
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Crystallization and preliminary crystallographic characterization of the iron-regulated outer membrane lipoprotein FrpD from Neisseria meningitidis
Author(s)	Sviridova, E. (CZ) Bumba, Ladislav (MBU-M)_{RID, ORCID} Řezáčová, Pavlína (UMG-J)_RID Procházková, Kateřina (UOCHB-X) Kavan, Daniel (MBU-M)_{RID, ORCID} Bezouška, Karel (MBU-M) Kutý, Michal (UEK-B) Šebo, Peter (MBU-M)_{RID, ORCID} Kutá-Smatanová, Ivana (UEK-B)_RID
Source Title	Acta Crystallographica Section F-Structural Biology and Crystallization Communications. - : Wiley - ISSN 1744-3091 Roč. 66, - (2010), s. 1119-1123
Number of pages	5 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	Fe-regulated protein D ; iron-regulated proteins ; outer membrane lipoproteins
Subject RIV	EC - Immunology
R&D Projects	LC06010 GA MŠMT - Ministry of Education, Youth and Sports (MEYS)
	GP310/06/P150 GA ČR - Czech Science Foundation (CSF)
CEZ	AV0Z50200510 - MBU-M (2005-2011)
	AV0Z50520514 - UMG-J (2005-2011)
	AV0Z60870520 - UEK-B (2005-2011)
	AV0Z40550506 - UOCHB-X (2005-2011)
UT WOS	000281635600035
DOI	10.1107/S174430911003215X
Annotation	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
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2011

Number of the records: 1