Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.
Structural insights into the elevator-type transport mechanism of a bacterial ZIP metal transporter.
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DOI:
10.1038/s41467-023-36048-4
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发表时间:
2023-01-24
影响因子:
16.6
通讯作者:
Hu, Jian
中科院分区:
文献类型:
--
作者:
Zhang, Yao;Jiang, Yuhan;Gao, Kaifu;Sui, Dexin;Yu, Peixuan;Su, Min;Wei, Guo-Wei;Hu, Jian
The Zrt-/Irt-like protein (ZIP) family consists of ubiquitously expressed divalent metal transporters critically involved in maintaining systemic and cellular homeostasis of zinc, iron, and manganese. Here, we present a study on a prokaryotic ZIP from Bordetella bronchiseptica (BbZIP) by combining structural biology, evolutionary covariance, computational modeling, and a variety of biochemical assays to tackle the issue of the transport mechanism which has not been established for the ZIP family. The apo state structure in an inward-facing conformation revealed a disassembled transport site, altered inter-helical interactions, and importantly, a rigid body movement of a 4-transmembrane helix (TM) bundle relative to the other TMs. The computationally generated and biochemically validated outward-facing conformation model revealed a slide of the 4-TM bundle, which carries the transport site(s), by approximately 8 Å toward the extracellular side against the static TMs which mediate dimerization. These findings allow us to conclude that BbZIP is an elevator-type transporter. The ZIP family (SLC39A) is involved in transition metal homeostasis. Here, authors use integrated approaches to conclude that the ZIP from Bordetella bronchiseptica (BbZIP) utilizes the elevator-type transport mechanism to achieve alternating access.
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DOI:
10.1073/pnas.1222142110
发表时间:
2013-06-11
影响因子:
11.1
作者:
Chowanadisai, Winyoo;Graham, David M.;Messerli, Mark A.
通讯作者:
Messerli, Mark A.
DOI:
10.1073/pnas.0804659105
发表时间:
2008-07-29
影响因子:
11.1
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通讯作者:
Rudnick, Gary
影响因子:
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通讯作者:
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影响因子:
6.7
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通讯作者:
Wilson D
影响因子:
2.9
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通讯作者:
Dempski, Robert E.