3hyr
From Proteopedia
Structural Insight into G Protein Coupling and Regulation of Fe2+ Membrane Transport
Structural highlights
FunctionFEOB_ECOLI GTP-driven Fe(2+) uptake system.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedG 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. Structural basis of GDP release and gating in G protein coupled Fe2+ transport.,Guilfoyle A, Maher MJ, Rapp M, Clarke R, Harrop S, Jormakka M EMBO J. 2009 Sep 2;28(17):2677-85. Epub 2009 Jul 23. PMID:19629046[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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