3HYT
Structural Basis of GDP Release and Gating in G Protein Coupled Fe2+ Transport
Summary for 3HYT
| Entry DOI | 10.2210/pdb3hyt/pdb |
| Related | 3HYR |
| Descriptor | Ferrous iron transport protein B, 2-amino-9-(5-O-[(R)-hydroxy{[(R)-hydroxy(phosphonoamino)phosphoryl]oxy}phosphoryl]-3-O-{[2-(methylamino)phenyl]carbonyl}-beta-D-erythro-pentofuranosyl-2-ulose)-1,9-dihydro-6H-purin-6-one, MAGNESIUM ION, ... (4 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 | 91174.71 |
| Authors | Maher, M.J.,Jormakka, M. (deposition date: 2009-06-23, release date: 2009-08-25, Last modification date: 2024-03-20) |
| 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 Fe(2+) transport. Embo J., 2009 Cited by 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: 19629046DOI: 10.1038/emboj.2009.208 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.74 Å) |
Structure validation
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