5AYO
Crystal structure of a bacterial homologue of iron transporter ferroportin in inward-facing state
5AYO の概要
| エントリーDOI | 10.2210/pdb5ayo/pdb |
| 関連するPDBエントリー | 5AYM 5AYN |
| 分子名称 | Solute carrier family 39 (Iron-regulated transporter), POTASSIUM ION, ZINC ION, ... (5 entities in total) |
| 機能のキーワード | alpha helical, transport protein |
| 由来する生物種 | Bdellovibrio bacteriovorus |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 49127.24 |
| 構造登録者 | Taniguchi, R.,Kato, H.E.,Font, J.,Deshpande, C.N.,Ishitani, R.,Jormakka, M.,Nureki, O. (登録日: 2015-08-25, 公開日: 2015-11-04, 最終更新日: 2024-03-20) |
| 主引用文献 | Taniguchi, R.,Kato, H.E.,Font, J.,Deshpande, C.N.,Wada, M.,Ito, K.,Ishitani, R.,Jormakka, M.,Nureki, O. Outward- and inward-facing structures of a putative bacterial transition-metal transporter with homology to ferroportin Nat Commun, 6:8545-8545, 2015 Cited by PubMed Abstract: In vertebrates, the iron exporter ferroportin releases Fe(2+) from cells into plasma, thereby maintaining iron homeostasis. The transport activity of ferroportin is suppressed by the peptide hormone hepcidin, which exhibits upregulated expression in chronic inflammation, causing iron-restrictive anaemia. However, due to the lack of structural information about ferroportin, the mechanisms of its iron transport and hepcidin-mediated regulation remain largely elusive. Here we report the crystal structures of a putative bacterial homologue of ferroportin, BbFPN, in both the outward- and inward-facing states. Despite undetectable sequence similarity, BbFPN adopts the major facilitator superfamily fold. A comparison of the two structures reveals that BbFPN undergoes an intra-domain conformational rearrangement during the transport cycle. We identify a substrate metal-binding site, based on structural and mutational analyses. Furthermore, the BbFPN structures suggest that a predicted hepcidin-binding site of ferroportin is located within its central cavity. Thus, BbFPN may be a valuable structural model for iron homeostasis regulation by ferroportin. PubMed: 26461048DOI: 10.1038/ncomms9545 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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