1lnq | pdb_00001lnq

CRYSTAL STRUCTURE OF MTHK AT 3.3 A

spinqualitylabelsall models 1lnq, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1lnq is a 8 chain structure with sequence from "methanobacterium_thermoautotrophicus"_(sic)_zeikus_and_wolfe_1972 "methanobacterium thermoautotrophicus" (sic) zeikus and wolfe 1972. The February 2003 RCSB PDB Molecule of the Month feature on Potassium Channels by Shuchismita Dutta and David S. Goodsell is 10.2210/rcsb_pdb/mom_2003_2. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA Gene: mth1520 ("Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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