6eo1

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m (Protected "6eo1" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 6eo1 is ON HOLD until Paper Publication
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==The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)==
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<StructureSection load='6eo1' size='340' side='right' caption='[[6eo1]], [[Resolution|resolution]] 4.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6eo1]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6EO1 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
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<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=6eo1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eo1 OCA], [http://pdbe.org/6eo1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eo1 RCSB], [http://www.ebi.ac.uk/pdbsum/6eo1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eo1 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Eukaryotic cyclic nucleotide-modulated channels perform their diverse physiological roles by opening and closing their pores to ions in response to cyclic nucleotide binding. We here present a structural model for the cyclic nucleotide-modulated potassium channel homolog from Mesorhizobium loti, MloK1, determined from 2D crystals in the presence of lipids. Even though crystals diffract electrons to only approximately 10 A, using cryoelectron microscopy (cryo-EM) and recently developed computational methods, we have determined a 3D map of full-length MloK1 in the presence of cyclic AMP (cAMP) at approximately 4.5 A isotropic 3D resolution. The structure provides a clear picture of the arrangement of the cyclic nucleotide-binding domains with respect to both the pore and the putative voltage sensor domains when cAMP is bound, and reveals a potential gating mechanism in the context of the lipid-embedded channel.
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Authors:
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High-Resolution Cryoelectron Microscopy Structure of the Cyclic Nucleotide-Modulated Potassium Channel MloK1 in a Lipid Bilayer.,Kowal J, Biyani N, Chami M, Scherer S, Rzepiela AJ, Baumgartner P, Upadhyay V, Nimigean CM, Stahlberg H Structure. 2017 Dec 1. pii: S0969-2126(17)30365-9. doi:, 10.1016/j.str.2017.11.012. PMID:29249605<ref>PMID:29249605</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6eo1" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Baumgartner, P]]
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[[Category: Biyani, N]]
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[[Category: Chami, M]]
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[[Category: Kowal, J]]
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[[Category: Nimigean, C]]
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[[Category: Rzepiela, A]]
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[[Category: Scherer, S]]
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[[Category: Stahlberg, H]]
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[[Category: Upadhyay, V]]
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[[Category: Cnbd]]
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[[Category: Cytoplasmic domain]]
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[[Category: Membrane protein]]
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[[Category: Mlok1]]
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[[Category: Mlotik1]]
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[[Category: Pco refinement]]
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[[Category: Potassium channel]]

Revision as of 08:43, 27 December 2017

The electron crystallography structure of the cAMP-bound potassium channel MloK1 (PCO-refined)

6eo1, resolution 4.50Å

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