6uzl
From Proteopedia
(Difference between revisions)
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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. 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 [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> |
</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='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> | ||
<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'>[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> | ||
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== 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] | [[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] | ||
| + | <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. | ||
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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®/PubMed®, 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__ | __TOC__ | ||
</SX> | </SX> | ||
| + | [[Category: Bacillus coli migula 1895]] | ||
[[Category: ABC-type lipid A-core oligosaccharide transporter]] | [[Category: ABC-type lipid A-core oligosaccharide transporter]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
Revision as of 10:29, 18 March 2020
Cryo-EM structure of nucleotide-free MsbA reconstituted into peptidiscs, conformation 2
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