4.8 Article

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

出版社

NATL ACAD SCIENCES
DOI: 10.1073/pnas.1612603113

关键词

X-ray structure; SLC4 transporter; | Bor1; Band 3; membrane protein

资金

  1. University of California Office of the President
  2. Multicampus Research Programs and Initiatives Grant [MR-15-338599]
  3. Program for Breakthrough Biomedical Research - Sandler Foundation
  4. National Institutes of Health [R37 GM024485]
  5. Alumni Fellow-Life Sciences Research Foundation fellowship

向作者/读者索取更多资源

Boron is essential for plant growth because of its incorporation into plant cellwalls; 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-angstrom 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.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.8
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据