4ei2: Difference between revisions

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{{STRUCTURE_4ei2| PDB=4ei2 | SCENE= }}
==Crystal Structures of MthK RCK gating ring bound to Barium==
===Crystal Structures of MthK RCK gating ring bound to Barium===
<StructureSection load='4ei2' size='340' side='right' caption='[[4ei2]], [[Resolution|resolution]] 3.11&Aring;' scene=''>
{{ABSTRACT_PUBMED_23085076}}
== Structural highlights ==
<table><tr><td colspan='2'>[[4ei2]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Metth Metth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EI2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4EI2 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=BA:BARIUM+ION'>BA</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3rbz|3rbz]], [[2fy8|2fy8]]</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">mthK, MTH_1520 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=187420 METTH])</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=4ei2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4ei2 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4ei2 RCSB], [http://www.ebi.ac.uk/pdbsum/4ei2 PDBsum]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH]] Calcium-gated potassium channel.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
RCK domains control activity of a variety of K(+) channels and transporters through binding of cytoplasmic ligands. To gain insight toward mechanisms of RCK domain activation, we solved the structure of the RCK domain from the Ca(2+)-gated K(+) channel, MthK, bound with Ba(2+), at 3.1 A resolution. The Ba(2+)-bound RCK domain was assembled as an octameric gating ring, as observed in structures of the full-length MthK channel, and shows Ba(2+) bound at several positions. One of the Ba(2+) sites, termed C1, overlaps with a known Ca(2+)-activation site, determined by residues D184 and E210. Functionally, Ba(2+) can activate reconstituted MthK channels as observed in electrophysiological recordings, whereas Mg(2+) (up to 100 mM) was ineffective. Ba(2+) activation was abolished by the mutation D184N, suggesting that Ba(2+) activates primarily through the C1 site. Our results suggest a working hypothesis for a sequence of ligand-dependent conformational changes that may underlie RCK domain activation and channel gating.


==Function==
Crystal Structure of a Ba(2+)-Bound Gating Ring Reveals Elementary Steps in RCK Domain Activation.,Smith FJ, Pau VP, Cingolani G, Rothberg BS Structure. 2012 Dec 5;20(12):2038-47. doi: 10.1016/j.str.2012.09.014. Epub 2012, Oct 18. PMID:23085076<ref>PMID:23085076</ref>
[[http://www.uniprot.org/uniprot/MTHK_METTH MTHK_METTH]] Calcium-gated potassium channel.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[4ei2]] is a 16 chain structure with sequence from [http://en.wikipedia.org/wiki/Metth Metth]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4EI2 OCA].
</div>


==See Also==
==See Also==
*[[Potassium Channel|Potassium Channel]]
*[[Potassium Channel|Potassium Channel]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:023085076</ref><references group="xtra"/><references/>
__TOC__
</StructureSection>
[[Category: Metth]]
[[Category: Metth]]
[[Category: Cingolani, G.]]
[[Category: Cingolani, G]]
[[Category: Rothberg, B S.]]
[[Category: Rothberg, B S]]
[[Category: Smith, F J.]]
[[Category: Smith, F J]]
[[Category: Ba2+ binding]]
[[Category: Ba2+ binding]]
[[Category: K+ channel]]
[[Category: K+ channel]]