Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila

Petermann, Nele; Hansen, Guido; Schmidt, Christian L.; Hilgenfeld, Rolf

doi:10.1016/j.febslet.2009.12.045

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Volume 584, Issue 4 , Pages 733-738, 19 February 2010

Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila

Edited by Richard Cogdell

Nele Petermann
- Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
Guido Hansen
- Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
Christian L. Schmidt
- Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
Rolf Hilgenfeld
- Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany
- Laboratory for Structural Biology of Infection and Inflammation, c/o DESY, Building 22a, Notkestr. 85, 22603 Hamburg, Germany
- Corresponding author. Address: Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Ratzeburger Allee 160, 23538 Lübeck, Germany. Fax: +49 451 500 4068.

Received 18 December 2009; accepted 21 December 2009. published online 25 December 2009.

Abstract

Prokaryotic pathogens have developed specialized mechanisms for efficient uptake of ferrous iron (Fe²⁺) from the host. In Legionella pneumophila, the causative agent of Legionnaires’ disease, the transmembrane GTPase FeoB plays a key role in Fe²⁺ acquisition and virulence. FeoB consists of a membrane-embedded core and an N-terminal, cytosolic region (NFeoB). Here, we report the crystal structure of NFeoB from L. pneumophila, revealing a monomeric protein comprising two separate domains with GTPase and guanine-nucleotide dissociation inhibitor (GDI) functions. The GDI domain displays a novel fold, whereas the overall structure of the GTPase domain resembles that of known G domains but is in the rarely observed nucleotide-free state.

Abbreviations: GDI, guanine-nucleotide dissociation inhibitor, HEPES, 4-(2-hydroxyethyl)-1-piperazineethanesulfonic acid, Tris, tris(hydroxymethyl) aminomethane

Keywords: Ferrous iron uptake, GTPase, GDI domain, X-ray structure, Legionella pneumophila