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1lss
From Proteopedia
Revision as of 15:28, 28 September 2014 by OCA (Talk | contribs)
1lss is a 4 chain structure with sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Roosild TP, Miller S, Booth IR, Choe S. A mechanism of regulating transmembrane potassium flux through a ligand-mediated conformational switch. Cell. 2002 Jun 14;109(6):781-91. PMID:12086676
