7Z6M
Crystal structure of Zn2+-transporter BbZIP in a cadmium bound state
7Z6M の概要
| エントリーDOI | 10.2210/pdb7z6m/pdb |
| 関連するPDBエントリー | 5TSA |
| 分子名称 | Putative membrane protein, CADMIUM ION (2 entities in total) |
| 機能のキーワード | zinc transporters, zrt/irt-like proteins (zips), solute carrier 39 (slc39) family, bbzip, transport mechanism, elevator mechanism, membrane protein, metal transport |
| 由来する生物種 | Bordetella bronchiseptica |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 33630.29 |
| 構造登録者 | Wiuf, A.,Steffen, J.H.,Becares, E.R.,Groenberg, C.,Mahato, D.R.,Rasmussen, S.G.F.,Andersson, M.,Croll, T.,Gotfryd, K.,Gourdon, P. (登録日: 2022-03-13, 公開日: 2022-08-10, 最終更新日: 2024-01-31) |
| 主引用文献 | Wiuf, A.,Steffen, J.H.,Becares, E.R.,Gronberg, C.,Mahato, D.R.,Rasmussen, S.G.F.,Andersson, M.,Croll, T.,Gotfryd, K.,Gourdon, P. The two-domain elevator-type mechanism of zinc-transporting ZIP proteins. Sci Adv, 8:eabn4331-eabn4331, 2022 Cited by PubMed Abstract: Zinc is essential for all organisms and yet detrimental at elevated levels. Hence, homeostasis of this metal is tightly regulated. The Zrt/Irt-like proteins (ZIPs) represent the only zinc importers in metazoans. Mutations in human ZIPs cause serious disorders, but the mechanism by which ZIPs transfer zinc remains elusive. Hitherto, structural information is only available for a model member, BbZIP, and as a single, ion-bound conformation, precluding mechanistic insights. Here, we elucidate an inward-open metal-free BbZIP structure, differing substantially in the relative positions of the two separate domains of ZIPs. With accompanying coevolutional analyses, mutagenesis, and uptake assays, the data point to an elevator-type transport mechanism, likely shared within the ZIP family, unifying earlier functional data. Moreover, the structure reveals a previously unknown ninth transmembrane segment that is important for activity in vivo. Our findings outline the mechanistic principles governing ZIP-protein transport and enhance the molecular understanding of ZIP-related disorders. PubMed: 35857505DOI: 10.1126/sciadv.abn4331 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.51 Å) |
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