3HYR

Structural Insight into G Protein Coupling and Regulation of Fe2+ Membrane Transport

Summary for 3HYR

• Entry DOI: 10.2210/pdb3hyr/pdb
• Related: 3HYT
• Descriptor: Ferrous iron transport protein B (2 entities in total)
• Functional Keywords: iron transport, g protein, cell inner membrane, cell membrane, gtp-binding, ion transport, iron, membrane, nucleotide-binding, transmembrane, transport, metal transport
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P33650
• Total number of polymer chains: 3
• Total formula weight: 89704.55

Authors

Maher, M.J.,Jormakka, M. (deposition date: 2009-06-23, release date: 2009-08-25, Last modification date: 2024-10-30)

Primary citation

Guilfoyle, A.,Maher, M.J.,Rapp, M.,Clarke, R.,Harrop, S.,Jormakka, M.
Structural basis of GDP release and gating in G protein coupled Fe2+ transport.
Embo J., 28:2677-2685, 2009

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.

PubMed: 19629046
DOI: 10.1038/emboj.2009.208

Experimental method

X-RAY DIFFRACTION (2.2 Å)