TY - JOUR
T1 - Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila
AU - Petermann, Nele
AU - Hansen, Guido
AU - Schmidt, Christian L.
AU - Hilgenfeld, Rolf
PY - 2010/2/1
Y1 - 2010/2/1
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.
UR - http://www.scopus.com/inward/record.url?scp=77649272520&partnerID=8YFLogxK
U2 - 10.1016/j.febslet.2009.12.045
DO - 10.1016/j.febslet.2009.12.045
M3 - Journal articles
C2 - 20036663
AN - SCOPUS:77649272520
SN - 0014-5793
VL - 584
SP - 733
EP - 738
JO - FEBS Letters
JF - FEBS Letters
IS - 4
ER -
