1lnq: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1lnq |SIZE=350|CAPTION= <scene name='initialview01'>1lnq</scene>, resolution 3.30Å | |PDB= 1lnq |SIZE=350|CAPTION= <scene name='initialview01'>1lnq</scene>, resolution 3.30Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= mth1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | |GENE= mth1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=145262 Methanothermobacter thermautotrophicus]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1lnq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1lnq RCSB]</span> | |||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Lee, A.]] | [[Category: Lee, A.]] | ||
[[Category: Mackinnon, R.]] | [[Category: Mackinnon, R.]] | ||
[[Category: helix bundle]] | [[Category: helix bundle]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
[[Category: rossman fold]] | [[Category: rossman fold]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:05:01 2008'' | ||
Revision as of 22:05, 30 March 2008
| |||||||
| , resolution 3.30Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | mth1520 (Methanothermobacter thermautotrophicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MTHK AT 3.3 A
OverviewOverview
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.
About this StructureAbout this Structure
1LNQ is a Single protein structure of sequence from Methanothermobacter thermautotrophicus. The following page contains interesting information on the relation of 1LNQ with [Potassium Channels]. Full crystallographic information is available from OCA.
ReferenceReference
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
Page seeded by OCA on Sun Mar 30 22:05:01 2008