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1lss

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(New page: 200px<br /><applet load="1lss" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lss, resolution 2.30&Aring;" /> '''KTN Mja218 CRYSTAL S...)
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[[Image:1lss.jpg|left|200px]]<br /><applet load="1lss" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1lss, resolution 2.30&Aring;" />
caption="1lss, resolution 2.30&Aring;" />
'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''<br />
'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''<br />
==Overview==
==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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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==
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1LSS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with NAD as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LSS OCA].
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1LSS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=NAD:'>NAD</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LSS OCA].
==Reference==
==Reference==
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[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Booth, I.R.]]
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[[Category: Booth, I R.]]
[[Category: Choe, S.]]
[[Category: Choe, S.]]
[[Category: Miller, S.]]
[[Category: Miller, S.]]
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[[Category: Roosild, T.P.]]
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[[Category: Roosild, T P.]]
[[Category: NAD]]
[[Category: NAD]]
[[Category: ktn domain]]
[[Category: ktn domain]]
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[[Category: rossman fold]]
[[Category: rossman fold]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:50:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:48:07 2008''

Revision as of 11:48, 21 February 2008

Image:1lss.jpg

1lss, resolution 2.30Å

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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 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 13:48:07 2008

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