Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila.
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.
Petermann
Nele
N
Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of Lübeck, Lübeck, Germany.
Hansen
Guido
G
Schmidt
Christian L
CL
Hilgenfeld
Rolf
R
D000595:Amino Acid Sequence; D001665:Binding Sites / Q000235:genetics; D020134:Catalytic Domain; D020558:GTP Phosphohydrolases / Q000378:metabolism; D020730:Guanine Nucleotide Dissociation Inhibitors / Q000378:metabolism; D007501:Iron / Q000378:metabolism*; D016952:Legionella pneumophila / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D026901:Membrane Transport Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017510:Protein Folding; D020836:Protein Structure, Quaternary; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D014961:X-Ray Diffraction
D020730:Guanine Nucleotide Dissociation Inhibitors; D026901:Membrane Transport Proteins; D007501:Iron; D020558:GTP Phosphohydrolases