Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila.,Petermann N, Hansen G, Schmidt CL, Hilgenfeld R FEBS Lett. 2010 Feb 19;584(4):733-8. Epub 2009 Dec 27. PMID:20036663[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Petermann N, Hansen G, Schmidt CL, Hilgenfeld R. Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila. FEBS Lett. 2010 Feb 19;584(4):733-8. Epub 2009 Dec 27. PMID:20036663 doi:10.1016/j.febslet.2009.12.045
