3IBY

Structure of cytosolic domain of L. pneumophila FeoB

Summary for 3IBY

• Entry DOI: 10.2210/pdb3iby/pdb
• Related: 3I8S 3I8X 3I92
• Descriptor: Ferrous iron transport protein B (2 entities in total)
• Functional Keywords: g protein, g domain, iron uptake, cell inner membrane, cell membrane, gtp-binding, ion transport, iron, iron transport, membrane, nucleotide-binding, transmembrane, transport, transport protein
• Biological source: Legionella pneumophila
• Cellular location: Cell inner membrane ; Multi-pass membrane protein : Q8GNS3
• Total number of polymer chains: 4
• Total formula weight: 113614.74

Authors

Petermann, N.,Hansen, G.,Hilgenfeld, R. (deposition date: 2009-07-17, release date: 2009-10-13, Last modification date: 2024-02-21)

Primary citation

Petermann, N.,Hansen, G.,Schmidt, C.L.,Hilgenfeld, R.
Structure of the GTPase and GDI domains of FeoB, the ferrous iron transporter of Legionella pneumophila.
Febs Lett., 584:733-738, 2010

PubMed Abstract: 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.

PubMed: 20036663
DOI: 10.1016/j.febslet.2009.12.045

Experimental method

X-RAY DIFFRACTION (2.5 Å)