4U9L
Structure of a membrane protein
4U9L の概要
エントリーDOI | 10.2210/pdb4u9l/pdb |
関連するPDBエントリー | 4U9N |
分子名称 | Magnesium transporter MgtE, MAGNESIUM ION, (2R)-2,3-dihydroxypropyl (9Z)-octadec-9-enoate, ... (4 entities in total) |
機能のキーワード | channel, magnesium, metal transport |
由来する生物種 | Thermus thermophilus HB8 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 40449.15 |
構造登録者 | Takeda, H.,Hattori, M.,Nishizawa, T.,Yamashita, K.,Shah, S.T.A.,Caffrey, M.,Maturana, A.D.,Ishitani, R.,Nureki, O. (登録日: 2014-08-06, 公開日: 2014-12-03, 最終更新日: 2024-03-20) |
主引用文献 | Takeda, H.,Hattori, M.,Nishizawa, T.,Yamashita, K.,Shah, S.T.,Caffrey, M.,Maturana, A.D.,Ishitani, R.,Nureki, O. Structural basis for ion selectivity revealed by high-resolution crystal structure of Mg(2+) channel MgtE Nat Commun, 5:5374-5374, 2014 Cited by PubMed Abstract: Magnesium is the most abundant divalent cation in living cells and is crucial to several biological processes. MgtE is a Mg(2+) channel distributed in all domains of life that contributes to the maintenance of cellular Mg(2+) homeostasis. Here we report the high-resolution crystal structures of the transmembrane domain of MgtE, bound to Mg(2+), Mn(2+) and Ca(2+). The high-resolution Mg(2+)-bound crystal structure clearly visualized the hydrated Mg(2+) ion within its selectivity filter. Based on those structures and biochemical analyses, we propose a cation selectivity mechanism for MgtE in which the geometry of the hydration shell of the fully hydrated Mg(2+) ion is recognized by the side-chain carboxylate groups in the selectivity filter. This is in contrast to the K(+)-selective filter of KcsA, which recognizes a dehydrated K(+) ion. Our results further revealed a cation-binding site on the periplasmic side, which regulate channel opening and prevents conduction of near-cognate cations. PubMed: 25367295DOI: 10.1038/ncomms6374 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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