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

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

*Korrespondierende/r Autor/-in für diese Arbeit
20 Zitate (Scopus)

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.

OriginalspracheEnglisch
ZeitschriftFEBS Letters
Jahrgang584
Ausgabenummer4
Seiten (von - bis)733-738
Seitenumfang6
ISSN0014-5793
DOIs
PublikationsstatusVeröffentlicht - 01.02.2010

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