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6uzl

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<SX load='6uzl' size='340' side='right' viewer='molstar' caption='[[6uzl]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
<SX load='6uzl' size='340' side='right' viewer='molstar' caption='[[6uzl]], [[Resolution|resolution]] 4.40&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<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>
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<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>
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</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>
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</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>
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<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>
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<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>
</table>
== Function ==
== Function ==
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[[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]
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[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.
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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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>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6uzl" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Escherichia coli]]
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[[Category: ABC-type lipid A-core oligosaccharide transporter]]
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[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Angiulli, G]]
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[[Category: Angiulli G]]
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[[Category: Dhupar, H S]]
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[[Category: Dhupar HS]]
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[[Category: Hoa, F Duong Van]]
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[[Category: Duong Van Hoa F]]
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[[Category: Suzuki, H]]
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[[Category: Suzuki H]]
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[[Category: Walz, T]]
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[[Category: Walz T]]
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[[Category: Wason, I S]]
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[[Category: Wason IS]]
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[[Category: Abc transporter]]
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[[Category: Membrane mimetic]]
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[[Category: Membrane protein]]
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[[Category: Peptidisc]]
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[[Category: Translocase]]
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Revision as of 14:34, 6 March 2024

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

6uzl, resolution 4.40Å

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