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2JLN

Structure of Mhp1, a nucleobase-cation-symport-1 family transporter

2JLN の概要
エントリーDOI10.2210/pdb2jln/pdb
関連するPDBエントリー2JLO
分子名称MHP1, SODIUM ION, MERCURY (II) ION (3 entities in total)
機能のキーワードhydantoin, transporter, membrane protein, nucleobase-cation-symport-1 family
由来する生物種MICROBACTERIUM LIQUEFACIENS
タンパク質・核酸の鎖数1
化学式量合計54842.37
構造登録者
主引用文献Weyand, S.,Shimamura, T.,Yajima, S.,Suzuki, S.,Mirza, O.,Krusong, K.,Carpenter, E.P.,Rutherford, N.G.,Hadden, J.M.,O'Reilly, J.,Ma, P.,Saidijam, M.,Patching, S.G.,Hope, R.J.,Norbertczak, H.T.,Roach, P.C.J.,Iwata, S.,Henderson, P.J.F.,Cameron, A.D.
Structure and Molecular Mechanism of a Nucleobase-Cation-Symport-1 Family Transporter.
Science, 322:709-, 2008
Cited by
PubMed Abstract: The nucleobase-cation-symport-1 (NCS1) transporters are essential components of salvage pathways for nucleobases and related metabolites. Here, we report the 2.85-angstrom resolution structure of the NCS1 benzyl-hydantoin transporter, Mhp1, from Microbacterium liquefaciens. Mhp1 contains 12 transmembrane helices, 10 of which are arranged in two inverted repeats of five helices. The structures of the outward-facing open and substrate-bound occluded conformations were solved, showing how the outward-facing cavity closes upon binding of substrate. Comparisons with the leucine transporter LeuT(Aa) and the galactose transporter vSGLT reveal that the outward- and inward-facing cavities are symmetrically arranged on opposite sides of the membrane. The reciprocal opening and closing of these cavities is synchronized by the inverted repeat helices 3 and 8, providing the structural basis of the alternating access model for membrane transport.
PubMed: 18927357
DOI: 10.1126/SCIENCE.1164440
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.85 Å)
構造検証レポート
Validation report summary of 2jln
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-02-04に公開中

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