6i9d: Difference between revisions

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'''Unreleased structure'''


The entry 6i9d is ON HOLD until Paper Publication
==MloK1 consensus structure from single particle analysis of 2D crystals==
<SX load='6i9d' size='340' side='right' viewer='molstar' caption='[[6i9d]], [[Resolution|resolution]] 4.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6i9d]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6I9D OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6I9D FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=K:POTASSIUM+ION'>K</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6iax|6iax]], [[6qcy|6qcy]], [[6qcz|6qcz]], [[6qd0|6qd0]], [[6qd1|6qd1]], [[6qd2|6qd2]], [[6qd3|6qd3]], [[6qd4|6qd4]]</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6i9d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6i9d OCA], [http://pdbe.org/6i9d PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6i9d RCSB], [http://www.ebi.ac.uk/pdbsum/6i9d PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6i9d ProSAT]</span></td></tr>
</table>
== Function ==
[[http://www.uniprot.org/uniprot/CNGK1_RHILO CNGK1_RHILO]] Cyclic nucleotide-regulated potassium channel activated by cAMP.<ref>PMID:15550244</ref>  
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Electron crystallography can reveal the structure of membrane proteins within 2D crystals under close-to-native conditions. High-resolution structural information can only be reached if crystals are perfectly flat and highly ordered. In practice, such crystals are difficult to obtain. Available image unbending algorithms correct for disorder, but only perform well on images of non-tilted, flat crystals, while out-of-plane distortions are not addressed. Here, we present an approach that employs single-particle refinement procedures to locally unbend crystals in 3D. With this method, density maps of the MloK1 potassium channel with a resolution of 4 A were obtained from images of 2D crystals that do not diffract beyond 10 A. Furthermore, 3D classification allowed multiple structures to be resolved, revealing a series of MloK1 conformations within a single 2D crystal. This conformational heterogeneity explains the poor diffraction observed and is related to channel function. The approach is implemented in the FOCUS package.


Authors: Righetto, R., Biyani, N., Kowal, J., Chami, M., Stahlberg, H.
Retrieving high-resolution information from disordered 2D crystals by single-particle cryo-EM.,Righetto RD, Biyani N, Kowal J, Chami M, Stahlberg H Nat Commun. 2019 Apr 12;10(1):1722. doi: 10.1038/s41467-019-09661-5. PMID:30979902<ref>PMID:30979902</ref>


Description: MloK1 consensus structure from single particle analysis of 2D crystals
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6i9d" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Large Structures]]
[[Category: Biyani, N]]
[[Category: Chami, M]]
[[Category: Chami, M]]
[[Category: Kowal, J]]
[[Category: Righetto, R]]
[[Category: Righetto, R]]
[[Category: Kowal, J]]
[[Category: Biyani, N]]
[[Category: Stahlberg, H]]
[[Category: Stahlberg, H]]
[[Category: Cyclic nucleotide-binding domain]]
[[Category: Ion channel]]
[[Category: Ion transport]]
[[Category: Membrane protein]]
[[Category: Voltage-gated potassium channel]]

Latest revision as of 04:40, 11 April 2020

MloK1 consensus structure from single particle analysis of 2D crystalsMloK1 consensus structure from single particle analysis of 2D crystals

6i9d, resolution 4.00Å

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