Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB

Kuo Wei Hung, Yi Wei Chang, Edward T. Eng, Jai Hui Chen, Yi Chung Chen, Yuh Ju Sun, Chwan Deng Hsiao, Gang Dong, Krasimir A. Spasov, Vinzenz M. Unger, Tai huang Huang

研究成果: 雜誌貢獻文章

21 引文 斯高帕斯(Scopus)

摘要

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.

原文英語
頁(從 - 到)501-512
頁數12
期刊Journal of Structural Biology
170
發行號3
DOIs
出版狀態已發佈 - 2010 六月 1

ASJC Scopus subject areas

  • Structural Biology

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    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. (2010). Structural fold, conservation and Fe(II) binding of the intracellular domain of prokaryote FeoB. Journal of Structural Biology, 170(3), 501-512. https://doi.org/10.1016/j.jsb.2010.01.017