1lss: Difference between revisions

Revision as of 22:04, 2 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1lss.png

Template:STRUCTURE 1lss

KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+

Template:ABSTRACT PUBMED 12086676

About this StructureAbout this Structure

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

ReferenceReference

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 Wed Jul 2 22:04:46 2008

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OCA

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-'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''
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-==Overview==
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-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.
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+{{ABSTRACT_PUBMED_12086676}}
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 [[Category: Rck domain]]
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