1LSS

KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+

1LSS の概要

• エントリーDOI: 10.2210/pdb1lss/pdb
• 関連するPDBエントリー: 1LSU
• 分子名称: Trk system potassium uptake protein trkA homolog, NICOTINAMIDE-ADENINE-DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: ktn domain, nad, rck domain, potassium transport, potassium channel, ktra, rossmann fold, transport protein
• 由来する生物種: Methanocaldococcus jannaschii
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 63524.10

構造登録者

Roosild, T.P.,Miller, S.,Booth, I.R.,Choe, S. (登録日: 2002-05-18, 公開日: 2002-07-03, 最終更新日: 2024-02-14)

主引用文献

Roosild, T.P.,Miller, S.,Booth, I.R.,Choe, S.
A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch.
Cell(Cambridge,Mass.), 109:781-791, 2002

PubMed Abstract: The regulation of cation content is critical for cell growth. However, the molecular mechanisms that gate the systems that control K+ movements remain unclear. KTN is a highly conserved cytoplasmic domain present ubiquitously in a variety of prokaryotic and eukaryotic K+ channels and transporters. Here we report crystal structures for two representative KTN domains that reveal a dimeric hinged assembly. Alternative ligands NAD+ and NADH block or vacate, respectively, the hinge region affecting the dimer's conformational flexibility. Conserved, surface-exposed hydrophobic patches that become coplanar upon hinge closure provide an assembly interface for KTN tetramerization. Mutational analysis using the KefC system demonstrates that this domain directly interacts with its respective transmembrane constituent, coupling ligand-mediated KTN conformational changes to the permease's activity.

PubMed: 12086676
DOI: 10.1016/S0092-8674(02)00768-7

実験手法

X-RAY DIFFRACTION (2.3 Å)