1lss: Difference between revisions

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


{{Structure
<!--
|PDB= 1lss |SIZE=350|CAPTION= <scene name='initialview01'>1lss</scene>, resolution 2.30&Aring;
The line below this paragraph, containing "STRUCTURE_1lss", creates the "Structure Box" on the page.
|SITE=
You may change the PDB parameter (which sets the PDB file loaded into the applet)
|LIGAND= <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene>
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
|ACTIVITY=  
or leave the SCENE parameter empty for the default display.
|GENE= KtrA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
-->
|DOMAIN=
{{STRUCTURE_1lss| PDB=1lss  | SCENE= }}  
|RELATEDENTRY=[[1lsu|1LSU]]
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lss OCA], [http://www.ebi.ac.uk/pdbsum/1lss PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lss RCSB]</span>
}}


'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''
'''KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+'''
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[[Category: Miller, S.]]
[[Category: Miller, S.]]
[[Category: Roosild, T P.]]
[[Category: Roosild, T P.]]
[[Category: ktn domain]]
[[Category: Ktn domain]]
[[Category: ktra]]
[[Category: Ktra]]
[[Category: nad]]
[[Category: Nad]]
[[Category: potassium channel]]
[[Category: Potassium channel]]
[[Category: potassium transport]]
[[Category: Potassium transport]]
[[Category: rck domain]]
[[Category: Rck domain]]
[[Category: rossman fold]]
[[Category: Rossman fold]]
 
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:06:54 2008''

Revision as of 00:15, 3 May 2008

File:1lss.jpg

Template:STRUCTURE 1lss

KTN Mja218 CRYSTAL STRUCTURE IN COMPLEX WITH NAD+


OverviewOverview

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 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 Sat May 3 00:15:08 2008

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