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

Petermann Nele | Zendy; Hansen Guido | Zendy; Schmidt Christian L. | Zendy; Hilgenfeld Rolf | Zendy

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

Author(s) -

Petermann Nele,

Hansen Guido,

Schmidt Christian L.,

Hilgenfeld Rolf

Publication year - 2010

Publication title -

febs letters

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.593

H-Index - 257

eISSN - 1873-3468

pISSN - 0014-5793

DOI - 10.1016/j.febslet.2009.12.045

Subject(s) - legionella pneumophila , gtpase , transmembrane domain , nucleotide , biology , transmembrane protein , biochemistry , legionella , transporter , ferrous , biophysics , dynamin , effector , chemistry , microbiology and biotechnology , bacteria , membrane , endocytosis , receptor , genetics , gene , organic chemistry

Prokaryotic pathogens have developed specialized mechanisms for efficient uptake of ferrous iron (Fe 2+ ) from the host. In Legionella pneumophila , the causative agent of Legionnaires’ disease, the transmembrane GTPase FeoB plays a key role in Fe 2+ 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.

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