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转铁蛋白结合蛋白 B 摄取转铁蛋白的结构基础。

The structural basis of transferrin sequestration by transferrin-binding protein B.

机构信息

Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada.

出版信息

Nat Struct Mol Biol. 2012 Feb 19;19(3):358-60. doi: 10.1038/nsmb.2251.

Abstract

Neisseria meningitidis, the causative agent of bacterial meningitis, acquires the essential element iron from the host glycoprotein transferrin during infection through a surface transferrin receptor system composed of proteins TbpA and TbpB. Here we present the crystal structures of TbpB from N. meningitidis in its apo form and in complex with human transferrin. The structure reveals how TbpB sequesters and initiates iron release from human transferrin.

摘要

脑膜炎奈瑟菌是细菌性脑膜炎的病原体,它通过由 TbpA 和 TbpB 蛋白组成的表面转铁蛋白受体系统从宿主糖蛋白转铁蛋白中获取感染过程中必需的元素铁。在此,我们展示了脑膜炎奈瑟菌 TbpB 在apo 形式和与人转铁蛋白复合物形式下的晶体结构。该结构揭示了 TbpB 如何螯合并启动人转铁蛋白中铁的释放。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/66f4/3981719/d249b44a09a0/nihms4091f1.jpg

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