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

doi:10.1016/j.febslet.2009.12.045

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

28 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.

Originalsprache	Englisch
Zeitschrift	FEBS Letters
Jahrgang	584
Ausgabenummer	4
Seiten (von - bis)	733-738
Seitenumfang	6
ISSN	0014-5793
DOIs	https://doi.org/10.1016/j.febslet.2009.12.045
Publikationsstatus	Veröffentlicht - 01.02.2010

Fördermittel

We thank T. Ursby (MAX-lab, Lund, Sweden) for assistance with synchrotron data collection, A. Wagner for her initial contributions to this project, and R. Wrase for support during the preparation of the manuscript. R.H. thanks the Fonds der Chemischen Industrie and the DFG Cluster of Excellence “Inflammation at Interfaces” for continuous support. Appendix A

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

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.",

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AU - Hansen, Guido

AU - Schmidt, Christian L.

AU - Hilgenfeld, Rolf

PY - 2010/2/1

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N2 - 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.

AB - 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.

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

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