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| | <SX load='6s8n' size='340' side='right' viewer='molstar' caption='[[6s8n]], [[Resolution|resolution]] 3.10Å' scene=''> | | <SX load='6s8n' size='340' side='right' viewer='molstar' caption='[[6s8n]], [[Resolution|resolution]] 3.10Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6s8n]] is a 5 chain structure with sequence from [http://en.wikipedia.org/wiki/"shigella_paradysenteriae"_weldin_1927 "shigella paradysenteriae" weldin 1927]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S8N OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6S8N FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6s8n]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Shigella_flexneri Shigella flexneri]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6S8N OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6S8N FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DCQ:2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-DIONE'>DCQ</scene>, <scene name='pdbligand=L0W:lipopolysaccharide+fragment'>L0W</scene>, <scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></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]] 3.1Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SGF_01136 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), lptC, SFxv_3552 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), lptF, SF4228, S4489 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), yjgQ, S4488, CQA91_25110, NCTC9783_00309, SAMEA3710568_03584 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927])</td></tr>
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DCQ:2-DECYL-5,6-DIMETHOXY-3-METHYLCYCLOHEXA-2,5-DIENE-1,4-DIONE'>DCQ</scene>, <scene name='pdbligand=L0W:lipopolysaccharide+fragment'>L0W</scene>, <scene name='pdbligand=LMN:LAURYL+MALTOSE+NEOPENTYL+GLYCOL'>LMN</scene>, <scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene></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=6s8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s8n OCA], [http://pdbe.org/6s8n PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6s8n RCSB], [http://www.ebi.ac.uk/pdbsum/6s8n PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6s8n 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=6s8n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6s8n OCA], [https://pdbe.org/6s8n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6s8n RCSB], [https://www.ebi.ac.uk/pdbsum/6s8n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6s8n ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LPTF_SHIFL LPTF_SHIFL]] Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. [[http://www.uniprot.org/uniprot/D2A8C1_SHIF2 D2A8C1_SHIF2]] Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. Facilitates the transfer of LPS from the inner membrane to the periplasmic protein LptA. Could be a docking site for LptA.[HAMAP-Rule:MF_01915] Required for the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane.[PIRNR:PIRNR028513] | + | [https://www.uniprot.org/uniprot/LPTB_SHIFL LPTB_SHIFL] Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (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__ |
| | </SX> | | </SX> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Chang, S H]] | + | [[Category: Shigella flexneri]] |
| - | [[Category: Dong, C J]] | + | [[Category: Chang SH]] |
| - | [[Category: Dong, H H]] | + | [[Category: Dong CJ]] |
| - | [[Category: Luo, Q H]] | + | [[Category: Dong HH]] |
| - | [[Category: Niu, Y]] | + | [[Category: Luo QH]] |
| - | [[Category: Qiao, W]] | + | [[Category: Niu Y]] |
| - | [[Category: Tang, X D]] | + | [[Category: Qiao W]] |
| - | [[Category: Wang, T]] | + | [[Category: Tang XD]] |
| - | [[Category: Xu, C H]] | + | [[Category: Wang T]] |
| - | [[Category: Yang, W X]] | + | [[Category: Xu CH]] |
| - | [[Category: Zhang, C B]] | + | [[Category: Yang WX]] |
| - | [[Category: Zhang, X]] | + | [[Category: Zhang CB]] |
| - | [[Category: Zhang, Z B]] | + | [[Category: Zhang X]] |
| - | [[Category: Zhang, Z Y]] | + | [[Category: Zhang ZB]] |
| - | [[Category: Zhu, X F]] | + | [[Category: Zhang ZY]] |
| - | [[Category: Abc transporter]]
| + | [[Category: Zhu XF]] |
| - | [[Category: Gram-negative bacteria]]
| + | |
| - | [[Category: Inner membrane protein complex]]
| + | |
| - | [[Category: Lipopolysaccharide transporter]]
| + | |
| - | [[Category: Lp]]
| + | |
| - | [[Category: Lptb]]
| + | |
| - | [[Category: Lptb2fgc]]
| + | |
| - | [[Category: Lptbfg]]
| + | |
| - | [[Category: Outer membrane]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
LPTB_SHIFL Part of the ABC transporter complex LptBFG involved in the translocation of lipopolysaccharide (LPS) from the inner membrane to the outer membrane. Probably responsible for energy coupling to the transport system (By similarity).
Publication Abstract from PubMed
Lipopolysaccharides (LPS) of Gram-negative bacteria are critical for the defence against cytotoxic substances and must be transported from the inner membrane (IM) to the outer membrane (OM) through a bridge formed by seven membrane proteins (LptBFGCADE). The IM component LptB2FG powers the process through a yet unclarified mechanism. Here we report three high-resolution cryo-EM structures of LptB2FG alone and complexed with LptC (LptB2FGC), trapped in either the LPS- or AMP-PNP-bound state. The structures reveal conformational changes between these states and substrate binding with or without LptC. We identify two functional transmembrane arginine-containing loops interacting with the bound AMP-PNP and elucidate allosteric communications between the domains. AMP-PNP binding induces an inward rotation and shift of the transmembrane helices of LptFG and LptC to tighten the cavity, with the closure of two lateral gates, to eventually expel LPS into the bridge. Functional assays reveal the functionality of the LptF and LptG periplasmic domains. Our findings shed light on the LPS transport mechanism.
Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism.,Tang X, Chang S, Luo Q, Zhang Z, Qiao W, Xu C, Zhang C, Niu Y, Yang W, Wang T, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H Nat Commun. 2019 Sep 13;10(1):4175. doi: 10.1038/s41467-019-11977-1. PMID:31519889[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tang X, Chang S, Luo Q, Zhang Z, Qiao W, Xu C, Zhang C, Niu Y, Yang W, Wang T, Zhang Z, Zhu X, Wei X, Dong C, Zhang X, Dong H. Cryo-EM structures of lipopolysaccharide transporter LptB2FGC in lipopolysaccharide or AMP-PNP-bound states reveal its transport mechanism. Nat Commun. 2019 Sep 13;10(1):4175. doi: 10.1038/s41467-019-11977-1. PMID:31519889 doi:http://dx.doi.org/10.1038/s41467-019-11977-1
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