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6uzl

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Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 2

6uzl, resolution 4.40Å

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 <SX load='6uzl' size='340' side='right' viewer='molstar' caption='[[6uzl]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6uzl]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UZL OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6UZL FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6uzl]] 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=6UZL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UZL FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/ABC-type_lipid_A-core_oligosaccharide_transporter ABC-type lipid A-core oligosaccharide transporter], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=7.5.2.6 7.5.2.6] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 4.4&#8491;</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=6uzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uzl OCA], [http://pdbe.org/6uzl PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6uzl RCSB], [http://www.ebi.ac.uk/pdbsum/6uzl PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6uzl ProSAT]</span></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=6uzl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uzl OCA], [https://pdbe.org/6uzl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uzl RCSB], [https://www.ebi.ac.uk/pdbsum/6uzl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uzl ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/C3TGA2_ECOLX C3TGA2_ECOLX]] 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.[HAMAP-Rule:MF_01703][SAAS:SAAS00055332]
+[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.
-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>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 6uzl" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </SX>
-[[Category: Bacillus coli migula 1895]]
+[[Category: Escherichia coli]]
-[[Category: ABC-type lipid A-core oligosaccharide transporter]]
 [[Category: Large Structures]]
-[[Category: Angiulli, G]]
+[[Category: Angiulli G]]
-[[Category: Dhupar, H S]]
+[[Category: Dhupar HS]]
-[[Category: Hoa, F Duong Van]]
+[[Category: Duong Van Hoa F]]
-[[Category: Suzuki, H]]
+[[Category: Suzuki H]]
-[[Category: Walz, T]]
+[[Category: Walz T]]
-[[Category: Wason, I S]]
+[[Category: Wason IS]]
-[[Category: Abc transporter]]
-[[Category: Membrane mimetic]]
-[[Category: Membrane protein]]
-[[Category: Peptidisc]]
-[[Category: Translocase]]

6uzl

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Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 2

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