2WIB : Crystal Structures of the N-terminal Intracellular Domain of FeoB from Klebsiella Pneumoniae in GDP binding state

  • Yi Chung Chen (Contributor)
  • Jai Hui Chen (Contributor)
  • Yi Wei Chang (Contributor)
  • Ying-Tsong Chen (Contributor)
  • Kuo Wei Hung (Contributor)
  • Yuh Ju Sun (Contributor)
  • Tai-Huang Huanga (Contributor)
  • Tai-huang Huang (Contributor)
  • Kuo Wei Hung (Contributor)
  • Chwan Deng Hsiao (Contributor)
  • Chwan Deng Hsiao (Contributor)

Dataset

Description

Experimental Technique/Method:X-RAY DIFFRACTION
Resolution:2.56
Classification:METAL TRANSPORT
Release Date:2010-05-19
Deposition Date:2009-05-09
Revision Date:2011-05-08#2011-07-13
Molecular Weight:59152.72
Macromolecule Type:Protein
Residue Count:534
Atom Site Count:3722
DOI:10.2210/pdb2wib/pdb

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.
Date made available2010 May 19
PublisherUnknown Publisher

Cite this