5N77

Crystal structure of the cytosolic domain of the CorA magnesium channel from Escherichia coli in complex with magnesium

5N77 の概要

• エントリーDOI: 10.2210/pdb5n77/pdb
• 分子名称: Magnesium transport protein CorA, MAGNESIUM ION, 2-(2-METHOXYETHOXY)ETHANOL, ... (4 entities in total)
• 機能のキーワード: homopentamer complex transport membrane, transport protein
• 由来する生物種: Escherichia coli
• 細胞内の位置: Cell inner membrane ; Multi-pass membrane protein : P0ABI4
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 149883.29

構造登録者

Lerche, M.,Sandhu, H.,Flockner, L.,Hogbom, M.,Rapp, M. (登録日: 2017-02-20, 公開日: 2017-07-12, 最終更新日: 2024-05-08)

主引用文献

Lerche, M.,Sandhu, H.,Flockner, L.,Hogbom, M.,Rapp, M.
Structure and Cooperativity of the Cytosolic Domain of the CorA Mg(2+) Channel from Escherichia coli.
Structure, 25:1175-1186.e4, 2017

PubMed Abstract: Structures of the Mg bound (closed) and apo (open) states of CorA suggests that channel gating is accomplished by rigid-body motions between symmetric and asymmetric assemblies of the cytosolic portions of the five subunits in response to ligand (Mg) binding/unbinding at interfacial sites. Here, we structurally and biochemically characterize the isolated cytosolic domain from Escherichia coli CorA. The data reveal an Mg-ligand binding site located in a novel position between each of the five subunits and two Mg ions trapped inside the pore. Soaking experiments show that cobalt hexammine outcompetes Mg at the pore site closest to the membrane. This represents the first structural information of how an analog of hexa-hydrated Mg (and competitive inhibitor of CorA) associates to the CorA pore. Biochemical data on the isolated cytoplasmic domain and full-length protein suggests that gating of the CorA channel is governed cooperatively.

PubMed: 28669631
DOI: 10.1016/j.str.2017.05.024

実験手法

X-RAY DIFFRACTION (2.8 Å)