2WIB

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

2WIB の概要

• エントリーDOI: 10.2210/pdb2wib/pdb
• 関連するPDBエントリー: 2WIA 2WIC
• 分子名称: FERROUS IRON TRANSPORT PROTEIN B, GUANOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: signal transduction, ferrous iron transport, membrane protein, metal transport, g protein
• 由来する生物種: KLEBSIELLA PNEUMONIAE
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59152.72

構造登録者

Hung, K.-W.,Chang, Y.-W.,Chen, J.-H.,Chen, Y.-C.,Sun, Y.-J.,Hsiao, C.-D.,Huang, T.-H. (登録日: 2009-05-09, 公開日: 2010-05-19, 最終更新日: 2024-05-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.56 Å)