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| | <SX load='6uzl' size='340' side='right' viewer='molstar' caption='[[6uzl]], [[Resolution|resolution]] 4.40Å' scene=''> | | <SX load='6uzl' size='340' side='right' viewer='molstar' caption='[[6uzl]], [[Resolution|resolution]] 4.40Å' scene=''> |
| | == Structural highlights == | | == 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://oca.weizmann.ac.il/oca-docs/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]] 4.4Å</td></tr> |
| - | <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=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> | | </table> |
| | == Function == | | == 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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Bacillus coli migula 1895]] | + | [[Category: Escherichia coli]] |
| - | [[Category: ABC-type lipid A-core oligosaccharide transporter]]
| + | |
| | [[Category: Large Structures]] | | [[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]]
| + | |
| Structural highlights
Function
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Angiulli G, Dhupar HS, Suzuki H, Wason IS, Duong Van Hoa F, Walz T. New approach for membrane protein reconstitution into peptidiscs and basis for their adaptability to different proteins. Elife. 2020 Mar 3;9. pii: 53530. doi: 10.7554/eLife.53530. PMID:32125274 doi:http://dx.doi.org/10.7554/eLife.53530
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