6bl6: Difference between revisions
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The | ==Crystallization of lipid A transporter MsbA from Salmonella typhimurium== | ||
<StructureSection load='6bl6' size='340' side='right'caption='[[6bl6]], [[Resolution|resolution]] 2.80Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6bl6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._LT2 Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6BL6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6BL6 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.8Å</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=6bl6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6bl6 OCA], [https://pdbe.org/6bl6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6bl6 RCSB], [https://www.ebi.ac.uk/pdbsum/6bl6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6bl6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/MSBA_SALTY MSBA_SALTY] 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 (By similarity). | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
MsbA is an essential ATP-binding cassette transporter in Gram-negative bacteria that transports lipid A and lipopolysaccharide from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. Here we report the X-ray structure of MsbA from Salmonella typhimurium at 2.8-A resolution in an inward-facing conformation after cocrystallization with lipid A and using a stabilizing facial amphiphile. The structure displays a large amplitude opening in the transmembrane portal, which is likely required for lipid A to pass from its site of synthesis into the protein-enclosed transport pathway. Putative lipid A density is observed further inside the transmembrane cavity, consistent with a trap and flip model. Additional electron density attributed to lipid A is observed near an outer surface cleft at the periplasmic ends of the transmembrane helices. These findings provide new structural insights into the lipid A transport pathway through comparative analysis with existing MsbA structures. | |||
Structural Insights into the Lipid A Transport Pathway in MsbA.,Padayatti PS, Lee SC, Stanfield RL, Wen PC, Tajkhorshid E, Wilson IA, Zhang Q Structure. 2019 Apr 25. pii: S0969-2126(19)30129-7. doi:, 10.1016/j.str.2019.04.007. PMID:31130486<ref>PMID:31130486</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: Padayatti | <div class="pdbe-citations 6bl6" style="background-color:#fffaf0;"></div> | ||
[[Category: Zhang | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] | |||
[[Category: Lee SC]] | |||
[[Category: Padayatti PS]] | |||
[[Category: Stanfield RL]] | |||
[[Category: Wilson IA]] | |||
[[Category: Zhang Q]] | |||
Latest revision as of 17:44, 4 October 2023
Crystallization of lipid A transporter MsbA from Salmonella typhimuriumCrystallization of lipid A transporter MsbA from Salmonella typhimurium
Structural highlights
FunctionMSBA_SALTY 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 (By similarity). Publication Abstract from PubMedMsbA is an essential ATP-binding cassette transporter in Gram-negative bacteria that transports lipid A and lipopolysaccharide from the cytoplasmic leaflet to the periplasmic leaflet of the inner membrane. Here we report the X-ray structure of MsbA from Salmonella typhimurium at 2.8-A resolution in an inward-facing conformation after cocrystallization with lipid A and using a stabilizing facial amphiphile. The structure displays a large amplitude opening in the transmembrane portal, which is likely required for lipid A to pass from its site of synthesis into the protein-enclosed transport pathway. Putative lipid A density is observed further inside the transmembrane cavity, consistent with a trap and flip model. Additional electron density attributed to lipid A is observed near an outer surface cleft at the periplasmic ends of the transmembrane helices. These findings provide new structural insights into the lipid A transport pathway through comparative analysis with existing MsbA structures. Structural Insights into the Lipid A Transport Pathway in MsbA.,Padayatti PS, Lee SC, Stanfield RL, Wen PC, Tajkhorshid E, Wilson IA, Zhang Q Structure. 2019 Apr 25. pii: S0969-2126(19)30129-7. doi:, 10.1016/j.str.2019.04.007. PMID:31130486[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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