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3
Enhanced Boron Tolerance in Plants Mediated by Bidirectional Transport Through Plasma Membrane Intrinsic Proteins.通过质膜内在蛋白双向转运介导的植物硼耐受性增强
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Crystal structures reveal the molecular basis of ion translocation in sodium/proton antiporters.晶体结构揭示钠离子/质子反向转运体中离子转运的分子基础。
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Bor1的结构支持SLC4阴离子交换蛋白的一种转运体运输机制。

Structure of Bor1 supports an elevator transport mechanism for SLC4 anion exchangers.

作者信息

Thurtle-Schmidt Bryan H, Stroud Robert M

机构信息

Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158.

Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94158

出版信息

Proc Natl Acad Sci U S A. 2016 Sep 20;113(38):10542-6. doi: 10.1073/pnas.1612603113. Epub 2016 Sep 6.

DOI:10.1073/pnas.1612603113
PMID:27601653
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5035872/
Abstract

Boron is essential for plant growth because of its incorporation into plant cell walls; however, in excess it is toxic to plants. Boron transport and homeostasis in plants is regulated in part by the borate efflux transporter Bor1, a member of the solute carrier (SLC) 4 transporter family with homology to the human bicarbonate transporter Band 3. Here, we present the 4.1-Å resolution crystal structure of Arabidopsis thaliana Bor1. The structure displays a dimeric architecture in which dimerization is mediated by centralized Gate domains. Comparisons with a structure of Band 3 in an outward-open state reveal that the Core domains of Bor1 have rotated inwards to achieve an occluded state. Further structural comparisons with UapA, a xanthine transporter from the nucleobase-ascorbate transporter family, show that the downward pivoting of the Core domains relative to the Gate domains may access an inward-open state. These results suggest that the SLC4, SLC26, and nucleobase-ascorbate transporter families all share an elevator transport mechanism in which alternating access is provided by Core domains that carry substrates across a membrane.

摘要

硼对植物生长至关重要,因为它会掺入植物细胞壁中;然而,过量的硼对植物有毒。植物中硼的运输和稳态部分受硼酸盐外流转运蛋白Bor1调节,Bor1是溶质载体(SLC)4转运蛋白家族的成员,与人类碳酸氢盐转运蛋白Band 3具有同源性。在此,我们展示了拟南芥Bor1的4.1埃分辨率晶体结构。该结构呈现出二聚体架构,其中二聚化由位于中央的门控结构域介导。与处于向外开放状态的Band 3结构进行比较发现,Bor1的核心结构域已向内旋转以达到封闭状态。与核碱基 - 抗坏血酸转运蛋白家族的黄嘌呤转运蛋白UapA进行进一步的结构比较表明,核心结构域相对于门控结构域向下枢转可能会进入向内开放状态。这些结果表明,SLC4、SLC26和核碱基 - 抗坏血酸转运蛋白家族都共享一种电梯运输机制,其中携带底物穿过膜的核心结构域提供交替通道。