3HYT

Structural basis of GDP release and gating in G protein coupled Fe(2+) transport.

(2009) EMBO J 

• PubMed: 19629046 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/emboj.2009.208
• Primary Citation of Related Structures:  
  3HYR, 3HYT


• PubMed Abstract: 
  

  G proteins are key molecular switches in the regulation of membrane protein function and signal transduction. The prokaryotic membrane protein FeoB is involved in G protein coupled Fe(2+) transport, and is unique in that the G protein is directly tethered to the membrane domain. Here, we report the structure of the soluble domain of FeoB, including the G protein domain, and its assembly into an unexpected trimer. Comparisons between nucleotide free and liganded structures reveal the closed and open state of a central cytoplasmic pore, respectively. In addition, these data provide the first observation of a conformational switch in the nucleotide-binding G5 motif, defining the structural basis for GDP release. From these results, structural parallels are drawn to eukaryotic G protein coupled membrane processes.

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Organizational Affiliation: 

Centenary Institute, Sydney, New South Wales, Australia.