Crystal structure and mechanism of a calcium-gated potassium channel
Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenge...
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| Veröffentlicht in: | Nature 2002-05, Vol.417 (6888), p.515-522 |
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| creator | MacKinnon, Roderick Jiang, Youxing Lee, Alice Chen, Jiayun Cadene, Martine Chait, Brian T |
| description | Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenger-gated channels) or membrane voltage (voltage-gated channels). Here we present the structural basis of ligand gating in a K
+
channel that opens in response to intracellular Ca
2+
. We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K
+
channel (MthK) from
Methanobacterium thermoautotrophicum
in the Ca
2+
-bound, opened state. Eight RCK domains (regulators of K
+
conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca
2+
binding in a simple manner to perform mechanical work to open the pore. |
| doi_str_mv | 10.1038/417515a |
| format | Article |
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+
channel that opens in response to intracellular Ca
2+
. We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K
+
channel (MthK) from
Methanobacterium thermoautotrophicum
in the Ca
2+
-bound, opened state. Eight RCK domains (regulators of K
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2+
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+
channel that opens in response to intracellular Ca
2+
. We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K
+
channel (MthK) from
Methanobacterium thermoautotrophicum
in the Ca
2+
-bound, opened state. Eight RCK domains (regulators of K
+
conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca
2+
binding in a simple manner to perform mechanical work to open the pore.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>Bacteriology</subject><subject>Biological and medical sciences</subject><subject>Calcium</subject><subject>Calcium - pharmacology</subject><subject>CRYSTAL STRUCTURE</subject><subject>Crystallography, X-Ray</subject><subject>Crystals</subject><subject>Electrical properties</subject><subject>Electrophysiology</subject><subject>Fundamental and applied biological sciences. 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Psychology</topic><topic>Humanities and Social Sciences</topic><topic>Ion Channel Gating - drug effects</topic><topic>Ligands</topic><topic>Lipid Bilayers - metabolism</topic><topic>MATERIALS SCIENCE</topic><topic>Methanobacterium - chemistry</topic><topic>Methanobacterium - genetics</topic><topic>Methanobacterium thermoautotrophicum</topic><topic>Microbiology</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>MthK protein</topic><topic>multidisciplinary</topic><topic>NATIONAL SYNCHROTRON LIGHT SOURCE</topic><topic>NSLS</topic><topic>PARTICLE ACCELERATORS</topic><topic>Permeability, membrane transport, intracellular transport</topic><topic>POTASSIUM</topic><topic>Potassium Channels, Calcium-Activated - chemistry</topic><topic>Potassium Channels, Calcium-Activated - genetics</topic><topic>Potassium Channels, Calcium-Activated - metabolism</topic><topic>Protein Structure, Quaternary</topic><topic>Protein Structure, 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Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MacKinnon, Roderick</au><au>Jiang, Youxing</au><au>Lee, Alice</au><au>Chen, Jiayun</au><au>Cadene, Martine</au><au>Chait, Brian T</au><aucorp>Brookhaven National Laboratory, National Synchrotron Light Source (US)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystal structure and mechanism of a calcium-gated potassium channel</atitle><jtitle>Nature</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>2002-05-30</date><risdate>2002</risdate><volume>417</volume><issue>6888</issue><spage>515</spage><epage>522</epage><pages>515-522</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>Ion channels exhibit two essential biophysical properties; that is, selective ion conduction, and the ability to gate-open in response to an appropriate stimulus. Two general categories of ion channel gating are defined by the initiating stimulus: ligand binding (neurotransmitter- or second-messenger-gated channels) or membrane voltage (voltage-gated channels). Here we present the structural basis of ligand gating in a K
+
channel that opens in response to intracellular Ca
2+
. We have cloned, expressed, analysed electrical properties, and determined the crystal structure of a K
+
channel (MthK) from
Methanobacterium thermoautotrophicum
in the Ca
2+
-bound, opened state. Eight RCK domains (regulators of K
+
conductance) form a gating ring at the intracellular membrane surface. The gating ring uses the free energy of Ca
2+
binding in a simple manner to perform mechanical work to open the pore.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>12037559</pmid><doi>10.1038/417515a</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0028-0836 |
| ispartof | Nature, 2002-05, Vol.417 (6888), p.515-522 |
| issn | 0028-0836 1476-4687 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_743153328 |
| source | MEDLINE; Nature; SpringerNature Journals |
| subjects | Amino Acid Sequence Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism Bacteriology Biological and medical sciences Calcium Calcium - pharmacology CRYSTAL STRUCTURE Crystallography, X-Ray Crystals Electrical properties Electrophysiology Fundamental and applied biological sciences. Psychology Humanities and Social Sciences Ion Channel Gating - drug effects Ligands Lipid Bilayers - metabolism MATERIALS SCIENCE Methanobacterium - chemistry Methanobacterium - genetics Methanobacterium thermoautotrophicum Microbiology Models, Molecular Molecular Sequence Data MthK protein multidisciplinary NATIONAL SYNCHROTRON LIGHT SOURCE NSLS PARTICLE ACCELERATORS Permeability, membrane transport, intracellular transport POTASSIUM Potassium Channels, Calcium-Activated - chemistry Potassium Channels, Calcium-Activated - genetics Potassium Channels, Calcium-Activated - metabolism Protein Structure, Quaternary Protein Structure, Tertiary Science Science (multidisciplinary) Sequence Alignment Structure-Activity Relationship Thermodynamics |
| title | Crystal structure and mechanism of a calcium-gated potassium channel |
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