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| | <StructureSection load='6o30' size='340' side='right'caption='[[6o30]], [[Resolution|resolution]] 4.47Å' scene=''> | | <StructureSection load='6o30' size='340' side='right'caption='[[6o30]], [[Resolution|resolution]] 4.47Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6o30]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_typhimurium"_loeffler_1892 "bacillus typhimurium" loeffler 1892]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O30 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6O30 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6o30]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium Salmonella enterica subsp. enterica serovar Typhimurium]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6O30 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6O30 FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">msbA, DD95_15660, EIL76_15590 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=90371 "Bacillus typhimurium" Loeffler 1892])</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 4.47Å</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'>[https://proteopedia.org/fgij/fg.htm?mol=6o30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o30 OCA], [https://pdbe.org/6o30 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6o30 RCSB], [https://www.ebi.ac.uk/pdbsum/6o30 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6o30 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=6o30 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6o30 OCA], [http://pdbe.org/6o30 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6o30 RCSB], [http://www.ebi.ac.uk/pdbsum/6o30 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6o30 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/A0A0K6RU95_SALTM A0A0K6RU95_SALTM]] 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_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;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus typhimurium loeffler 1892]] | |
| - | [[Category: ABC-type lipid A-core oligosaccharide transporter]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lee, S C]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium]] |
| - | [[Category: Padayatti, P S]] | + | [[Category: Lee SC]] |
| - | [[Category: Stanfield, R L]] | + | [[Category: Padayatti PS]] |
| - | [[Category: Wilson, I A]] | + | [[Category: Stanfield RL]] |
| - | [[Category: Zhang, Q]] | + | [[Category: Wilson IA]] |
| - | [[Category: Abc transporter]] | + | [[Category: Zhang Q]] |
| - | [[Category: Lipid a co-crystallization]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Msba]]
| + | |
| - | [[Category: Staphylococcus typhimurium]]
| + | |
| Structural highlights
Function
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).
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Padayatti PS, Lee SC, Stanfield RL, Wen PC, Tajkhorshid E, Wilson IA, Zhang Q. Structural Insights into the Lipid A Transport Pathway in MsbA. Structure. 2019 Apr 25. pii: S0969-2126(19)30129-7. doi:, 10.1016/j.str.2019.04.007. PMID:31130486 doi:http://dx.doi.org/10.1016/j.str.2019.04.007
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