2H2P
Crystal structure of CLC-ec1 in complex with Fab fragment in SeCN-
2H2P の概要
エントリーDOI | 10.2210/pdb2h2p/pdb |
関連するPDBエントリー | 1OTS 2H2S |
分子名称 | CLC Cl transporter, FAB fragment, heavy chain, FAB fragment, light chain, ... (4 entities in total) |
機能のキーワード | clc; transporter; chloride; antiport, ion transport |
由来する生物種 | Escherichia coli 詳細 |
細胞内の位置 | Cell inner membrane ; Multi- pass membrane protein : P37019 |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 193721.93 |
構造登録者 | |
主引用文献 | Nguitragool, W.,Miller, C. Uncoupling of a CLC Cl(-)/H(+) Exchange Transporter by Polyatomic Anions J.Mol.Biol., 362:682-690, 2006 Cited by PubMed Abstract: CLC-ec1 is a bacterial archetype of CLC transporters, a ubiquitous class of proteins that catalyze transmembrane exchange of Cl- and H+ necessary for pH regulation of numerous physiological processes. Despite a profusion of high-resolution structures, the molecular mechanism of exchange remains unknown. Here, we rigorously demonstrate strict exchange stoichiometry of 2 Cl-/1 H+. In addition to Cl- and Br-, two non-halide ions, NO3- and SCN-, are shown to be transported by CLC-ec1, but with reduced H+ counter-transport. The loss of proton coupling to these anions is accompanied by an absence of bound anions in the central and external Cl- binding sites in the protein's anion selectivity region, as revealed by crystallographic comparison of Br- and SeCN- bound to this region. PubMed: 16905147DOI: 10.1016/j.jmb.2006.07.006 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.1 Å) |
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