1lss

From Proteopedia

Revision as of 18:43, 20 November 2007

KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+

Overview

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.

About this Structure

1LSS is a Single protein structure of sequence from Methanocaldococcus jannaschii with NAD as ligand. Full crystallographic information is available from OCA.

Reference

A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch., Roosild TP, Miller S, Booth IR, Choe S, Cell. 2002 Jun 14;109(6):781-91. PMID:12086676

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