2WIB

Crystal Structures of the N-terminal Intracellular Domain of FeoB from Klebsiella Pneumoniae in GDP binding state

Summary for 2WIB

• Entry DOI: 10.2210/pdb2wib/pdb
• Related: 2WIA 2WIC
• Descriptor: FERROUS IRON TRANSPORT PROTEIN B, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: signal transduction, ferrous iron transport, membrane protein, metal transport, g protein
• Biological source: KLEBSIELLA PNEUMONIAE
• Total number of polymer chains: 2
• Total formula weight: 59152.72

Authors

Hung, K.-W.,Chang, Y.-W.,Chen, J.-H.,Chen, Y.-C.,Sun, Y.-J.,Hsiao, C.-D.,Huang, T.-H. (deposition date: 2009-05-09, release date: 2010-05-19, Last modification date: 2024-05-01)

Primary citation

Hung, K.-W.,Chang, Y.-W.,Eng, E.T.,Chen, J.-H.,Chen, Y.-C.,Sun, Y.-J.,Hsiao, C.-D.,Dong, G.,Spasov, K.A.,Unger, V.M.,Huang, T.-H.
Structural Fold, Conservation and Fe(II) Binding of the Intracellular Domain of Prokaryote Feob.
J.Struct.Biol., 170:501-, 2010

PubMed Abstract: FeoB is a G-protein coupled membrane protein essential for Fe(II) uptake in prokaryotes. Here, we report the crystal structures of the intracellular domain of FeoB (NFeoB) from Klebsiella pneumoniae (KpNFeoB) and Pyrococcus furiosus (PfNFeoB) with and without bound ligands. In the structures, a canonical G-protein domain (G domain) is followed by a helical bundle domain (S-domain), which despite its lack of sequence similarity between species is structurally conserved. In the nucleotide-free state, the G-domain's two switch regions point away from the binding site. This gives rise to an open binding pocket whose shallowness is likely to be responsible for the low nucleotide-binding affinity. Nucleotide binding induced significant conformational changes in the G5 motif which in the case of GMPPNP binding was accompanied by destabilization of the switch I region. In addition to the structural data, we demonstrate that Fe(II)-induced foot printing cleaves the protein close to a putative Fe(II)-binding site at the tip of switch I, and we identify functionally important regions within the S-domain. Moreover, we show that NFeoB exists as a monomer in solution, and that its two constituent domains can undergo large conformational changes. The data show that the S-domain plays important roles in FeoB function.

PubMed: 20123128
DOI: 10.1016/J.JSB.2010.01.017

Experimental method

X-RAY DIFFRACTION (2.56 Å)