1lnq: Difference between revisions
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==CRYSTAL STRUCTURE OF MTHK AT 3.3 A== | ==CRYSTAL STRUCTURE OF MTHK AT 3.3 A== | ||
<StructureSection load='1lnq' size='340' side='right' caption='[[1lnq]], [[Resolution|resolution]] 3.30Å' scene=''> | <StructureSection load='1lnq' size='340' side='right' caption='[[1lnq]], [[Resolution|resolution]] 3.30Å' scene=''> | ||
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mth1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 "Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972])</td></tr> | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mth1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 "Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lnq OCA], [http://pdbe.org/1lnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lnq RCSB], [http://www.ebi.ac.uk/pdbsum/1lnq PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1lnq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lnq OCA], [http://pdbe.org/1lnq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1lnq RCSB], [http://www.ebi.ac.uk/pdbsum/1lnq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1lnq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1lnq_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ln/1lnq_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
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</div> | </div> | ||
<div class="pdbe-citations 1lnq" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1lnq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:41, 31 January 2018
CRYSTAL STRUCTURE OF MTHK AT 3.3 ACRYSTAL STRUCTURE OF MTHK AT 3.3 A
Structural highlights
Function[MTHK_METTH] Calcium-gated potassium channel. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIon 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. Crystal structure and mechanism of a calcium-gated potassium channel.,Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R Nature. 2002 May 30;417(6888):515-22. PMID:12037559[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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