1lsu
From Proteopedia
(New page: 200px<br /><applet load="1lsu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lsu, resolution 2.85Å" /> '''KTN Bsu222 Crystal S...) |
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| - | [[Image:1lsu.gif|left|200px]]<br /><applet load="1lsu" size=" | + | [[Image:1lsu.gif|left|200px]]<br /><applet load="1lsu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1lsu, resolution 2.85Å" /> | caption="1lsu, resolution 2.85Å" /> | ||
'''KTN Bsu222 Crystal Structure in Complex with NADH'''<br /> | '''KTN Bsu222 Crystal Structure in Complex with NADH'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The regulation of cation content is critical for cell growth. However, the | + | 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== | ==About this Structure== | ||
| - | 1LSU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with NAI as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1LSU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_subtilis Bacillus subtilis] with <scene name='pdbligand=NAI:'>NAI</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Bacillus subtilis]] | [[Category: Bacillus subtilis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Booth, I | + | [[Category: Booth, I R.]] |
[[Category: Choe, S.]] | [[Category: Choe, S.]] | ||
[[Category: Miller, S.]] | [[Category: Miller, S.]] | ||
| - | [[Category: Roosild, T | + | [[Category: Roosild, T P.]] |
[[Category: NAI]] | [[Category: NAI]] | ||
[[Category: ktn domain]] | [[Category: ktn domain]] | ||
| Line 26: | Line 26: | ||
[[Category: rossman fold]] | [[Category: rossman fold]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:06 2008'' |
Revision as of 11:48, 21 February 2008
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KTN Bsu222 Crystal Structure in Complex with NADH
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
1LSU is a Single protein structure of sequence from Bacillus subtilis with 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
Page seeded by OCA on Thu Feb 21 13:48:06 2008
Categories: Bacillus subtilis | Single protein | Booth, I R. | Choe, S. | Miller, S. | Roosild, T P. | NAI | Ktn domain | Ktra | Nad | Potassium channel | Potassium transport | Rck domain | Rossman fold
