Structural basis of GDP release and gating in G protein coupled Fe2 transport
Amy Guilfoyle, Megan J Maher, Mikaela Rapp, Ronald Clarke, Stephen Harrop, Mika Jormakka
The EMBO Journal | WILEY | Published : 2009
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 basi..View full abstract
Awarded by Australian Research Council
This study was supported by the Australian Research Council (ARC; DP0666970 to MJ). MR was a recipient of the Australian Research Council Linkage Fellowship (LX0881956) and supported by Stiftelsen Bengt Lundqvist Minne. MJM was supported by a Cancer Institute of NSW Career Development Fellowship. Data collection was done at the Advanced Photon Source (APS). We acknowledge the support of S Corcoran, N Venugopolan, and M Becker at GM/CA-CAT, for scientific support and assistance with data collection. GM/CA-CAT beamline (ID23) is supported by the US National Cancer Institute and the US National Institute of General Medical Science. Visits to APS were supported by the Australian Nuclear Science Technology Organization (ANSTO). This research was facilitated by access to the Sydney University Proteome Research Unit, established under the Australian Government's Major National Research Facilities program and supported by the University of Sydney. G von Heijne is acknowledged for supplying the FeoB-GFP vector and B Crossett for mass spectrometry. We thank Jeff Abramson and Gunnar von Heijne for critical assessment of the paper.