6bl6
From Proteopedia
(Difference between revisions)
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- | ==Crystallization of lipid A transporter MsbA from Salmonella typhimurium | + | ==Crystallization of lipid A transporter MsbA from Salmonella typhimurium== |
- | <StructureSection load='6bl6' size='340' side='right' caption='[[6bl6]], [[Resolution|resolution]] 2.80Å' scene=''> | + | <StructureSection load='6bl6' size='340' side='right'caption='[[6bl6]], [[Resolution|resolution]] 2.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6bl6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BL6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[6bl6]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Salty Salty]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6BL6 FirstGlance]. <br> | ||
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== Function == | == Function == | ||
[[http://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). | [[http://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. | ||
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+ | 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> | ||
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+ | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
+ | </div> | ||
+ | <div class="pdbe-citations 6bl6" style="background-color:#fffaf0;"></div> | ||
+ | == References == | ||
+ | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
+ | [[Category: Large Structures]] | ||
[[Category: Salty]] | [[Category: Salty]] | ||
[[Category: Lee, S C]] | [[Category: Lee, S C]] | ||
[[Category: Padayatti, P S]] | [[Category: Padayatti, P S]] | ||
+ | [[Category: Stanfield, R L]] | ||
[[Category: Wilson, I A]] | [[Category: Wilson, I A]] | ||
[[Category: Zhang, Q]] | [[Category: Zhang, Q]] |
Revision as of 06:08, 12 June 2019
Crystallization of lipid A transporter MsbA from Salmonella typhimurium
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