1lss: Difference between revisions

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[[Image:1lss.~~jpg~~|left|200px]]

[[Image:1lss.png|left|200px]]

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

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_12086676}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 12086676 is the PubMed ID number.

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==About this Structure==

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[[Category: Rck domain]]

[[Category: Rossman fold]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May~~ ~~3 00~~:15:08 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 22:04:46 2008''

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-[[Image:1lss.jpg|left|200px]]
+{{Seed}}
+[[Image:1lss.png|left|200px]]
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 {{STRUCTURE_1lss|  PDB=1lss  |  SCENE=  }}
-'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_12086676}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 12086676 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_12086676}}
 ==About this Structure==
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 [[Category: Rck domain]]
 [[Category: Rossman fold]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 00:15:08 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul  2 22:04:46 2008''