2nlj: Difference between revisions
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[[Image:2nlj.gif|left|200px]] | [[Image:2nlj.gif|left|200px]] | ||
'''Potassium Channel KcsA(M96V)-Fab complex in KCl''' | {{Structure | ||
|PDB= 2nlj |SIZE=350|CAPTION= <scene name='initialview01'>2nlj</scene>, resolution 2.520Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=K:POTASSIUM+ION'>K</scene> and <scene name='pdbligand=DGA:DIACYL GLYCEROL'>DGA</scene> | |||
|ACTIVITY= | |||
|GENE= kcsA, skc1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1916 Streptomyces lividans]) | |||
}} | |||
'''Potassium Channel KcsA(M96V)-Fab complex in KCl''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
2NLJ is a [ | 2NLJ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] and [http://en.wikipedia.org/wiki/Streptomyces_lividans Streptomyces lividans]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLJ OCA]. | ||
==Reference== | ==Reference== | ||
Structural and thermodynamic properties of selective ion binding in a K+ channel., Lockless SW, Zhou M, MacKinnon R, PLoS Biol. 2007 May;5(5):e121. PMID:[http:// | Structural and thermodynamic properties of selective ion binding in a K+ channel., Lockless SW, Zhou M, MacKinnon R, PLoS Biol. 2007 May;5(5):e121. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17472437 17472437] | ||
[[Category: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: voltage-gated channel]] | [[Category: voltage-gated channel]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:47:58 2008'' | ||
Revision as of 18:47, 20 March 2008
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| , resolution 2.520Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | and | ||||||
| Gene: | kcsA, skc1 (Streptomyces lividans) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Potassium Channel KcsA(M96V)-Fab complex in KCl
OverviewOverview
Thermodynamic measurements of ion binding to the Streptomyces lividans K(+) channel were carried out using isothermal titration calorimetry, whereas atomic structures of ion-bound and ion-free conformations of the channel were characterized by x-ray crystallography. Here we use these assays to show that the ion radius dependence of selectivity stems from the channel's recognition of ion size (i.e., volume) rather than charge density. Ion size recognition is a function of the channel's ability to adopt a very specific conductive structure with larger ions (K(+), Rb(+), Cs(+), and Ba(2+)) bound and not with smaller ions (Na(+), Mg(2+), and Ca(2+)). The formation of the conductive structure involves selectivity filter atoms that are in direct contact with bound ions as well as protein atoms surrounding the selectivity filter up to a distance of 15 A from the ions. We conclude that ion selectivity in a K(+) channel is a property of size-matched ion binding sites created by the protein structure.
About this StructureAbout this Structure
2NLJ is a Single protein structure of sequence from Mus musculus and Streptomyces lividans. Full crystallographic information is available from OCA.
ReferenceReference
Structural and thermodynamic properties of selective ion binding in a K+ channel., Lockless SW, Zhou M, MacKinnon R, PLoS Biol. 2007 May;5(5):e121. PMID:17472437
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