1lss
From Proteopedia
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| , resolution 2.30Å | |||||||
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| Ligands: | |||||||
| Gene: | KtrA (Methanocaldococcus jannaschii) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 12:34:44 2008
