1lnq

From Proteopedia

(Difference between revisions)

Revision as of 01:25, 10 September 2015

CRYSTAL STRUCTURE OF MTHK AT 3.3 A

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:
Gene:	mth1520 ("Methanobacterium thermoautotrophicus" (sic) Zeikus and Wolfe 1972)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R. Crystal structure and mechanism of a calcium-gated potassium channel. Nature. 2002 May 30;417(6888):515-22. PMID:12037559 doi:10.1038/417515a

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1lnq"

@@ Line 5: / Line 5: @@
 </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='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://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]</span></td></tr>
 </table>
 == Function ==
@@ Line 27: / Line 27: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1lnq" style="background-color:#fffaf0;"></div>
 ==See Also==

1lnq

From Proteopedia

Revision as of 01:25, 10 September 2015

CRYSTAL STRUCTURE OF MTHK AT 3.3 A

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox