6uz2: Difference between revisions

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'''Unreleased structure'''


The entry 6uz2 is ON HOLD  until Paper Publication
==Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 1==
<SX load='6uz2' size='340' side='right' viewer='molstar' caption='[[6uz2]], [[Resolution|resolution]] 4.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uz2]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UZ2 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UZ2 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.2&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6uz2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uz2 OCA], [https://pdbe.org/6uz2 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uz2 RCSB], [https://www.ebi.ac.uk/pdbsum/6uz2 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uz2 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MSBA_ECOLI MSBA_ECOLI] Involved in lipid A export and possibly also in glycerophospholipid export and for biogenesis of the outer membrane. Transmembrane domains (TMD) form a pore in the inner membrane and the ATP-binding domain (NBD) is responsible for energy generation.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Previously we introduced peptidiscs as an alternative to detergents to stabilize membrane proteins in solution (Carlson et al., 2018). Here, we present 'on-gradient' reconstitution, a new gentle approach for the reconstitution of labile membrane-protein complexes, and used it to reconstitute Rhodobacter sphaeroides reaction center complexes, demonstrating that peptidiscs can adapt to transmembrane domains of very different sizes and shapes. Using the conventional 'on-bead' approach, we reconstituted Escherichia coli proteins MsbA and MscS and find that peptidiscs stabilize them in their native conformation and allow for high-resolution structure determination by cryo-electron microscopy. The structures reveal that peptidisc peptides can arrange around transmembrane proteins differently, thus revealing the structural basis for why peptidiscs can stabilize such a large variety of membrane proteins. Together, our results establish the gentle and easy-to-use peptidiscs as a potentially universal alternative to detergents as a means to stabilize membrane proteins in solution for structural and functional studies.


Authors:  
New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins.,Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, Walz T Elife. 2020 Mar 3;9. pii: 53530. doi: 10.7554/eLife.53530. PMID:32125274<ref>PMID:32125274</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6uz2" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</SX>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Angiulli G]]
[[Category: Dhupar HS]]
[[Category: Duong Van Hoa F]]
[[Category: Suzuki H]]
[[Category: Walz T]]
[[Category: Wason IS]]

Latest revision as of 05:57, 14 May 2025

Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 1

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