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| | <StructureSection load='4n4r' size='340' side='right'caption='[[4n4r]], [[Resolution|resolution]] 2.80Å' scene=''> | | <StructureSection load='4n4r' size='340' side='right'caption='[[4n4r]], [[Resolution|resolution]] 2.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4n4r]] is a 4 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=4N4R OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4N4R FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4n4r]] is a 4 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=4N4R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4N4R FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CAC:CACODYLATE+ION'>CAC</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr> |
| - | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></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=4n4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4r OCA], [https://pdbe.org/4n4r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4n4r RCSB], [https://www.ebi.ac.uk/pdbsum/4n4r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4r ProSAT]</span></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">imp, lptD, ostA, STM0093 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY]), lptE, rlpB, STM0647 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=99287 SALTY])</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=4n4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4n4r OCA], [http://pdbe.org/4n4r PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4n4r RCSB], [http://www.ebi.ac.uk/pdbsum/4n4r PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4n4r ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LPTD_SALTY LPTD_SALTY]] Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (By similarity). [[http://www.uniprot.org/uniprot/LPTE_SALTY LPTE_SALTY]] Together with LptD, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane. Required for the proper assembly of LptD. Binds LPS and may serve as the LPS recognition site at the outer membrane (By similarity). | + | [https://www.uniprot.org/uniprot/LPTD_SALTY LPTD_SALTY] Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (By similarity). |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Salty]] | + | [[Category: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2]] |
| - | [[Category: Dong, C]] | + | [[Category: Dong C]] |
| - | [[Category: Dong, H]] | + | [[Category: Dong H]] |
| - | [[Category: He, C]] | + | [[Category: He C]] |
| - | [[Category: Paterson, N G]] | + | [[Category: Paterson NG]] |
| - | [[Category: Wang, W]] | + | [[Category: Wang W]] |
| - | [[Category: Wang, Z]] | + | [[Category: Wang Z]] |
| - | [[Category: Xiang, Q]] | + | [[Category: Xiang Q]] |
| - | [[Category: Zhang, Y]] | + | [[Category: Zhang Y]] |
| - | [[Category: Beta barrel]]
| + | |
| - | [[Category: Lipopolysaccharide transport protein]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Translocase]]
| + | |
| Structural highlights
Function
LPTD_SALTY Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (By similarity).
Publication Abstract from PubMed
Lipopolysaccharide (LPS) is essential for most Gram-negative bacteria and has crucial roles in protection of the bacteria from harsh environments and toxic compounds, including antibiotics. Seven LPS transport proteins (that is, LptA-LptG) form a trans-envelope protein complex responsible for the transport of LPS from the inner membrane to the outer membrane, the mechanism for which is poorly understood. Here we report the first crystal structure of the unique integral membrane LPS translocon LptD-LptE complex. LptD forms a novel 26-stranded beta-barrel, which is to our knowledge the largest beta-barrel reported so far. LptE adopts a roll-like structure located inside the barrel of LptD to form an unprecedented two-protein 'barrel and plug' architecture. The structure, molecular dynamics simulations and functional assays suggest that the hydrophilic O-antigen and the core oligosaccharide of the LPS may pass through the barrel and the lipid A of the LPS may be inserted into the outer leaflet of the outer membrane through a lateral opening between strands beta1 and beta26 of LptD. These findings not only help us to understand important aspects of bacterial outer membrane biogenesis, but also have significant potential for the development of novel drugs against multi-drug resistant pathogenic bacteria.
Structural basis for outer membrane lipopolysaccharide insertion.,Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C Nature. 2014 Jul 3;511(7507):52-6. doi: 10.1038/nature13464. Epub 2014 Jun 18. PMID:24990744[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Dong H, Xiang Q, Gu Y, Wang Z, Paterson NG, Stansfeld PJ, He C, Zhang Y, Wang W, Dong C. Structural basis for outer membrane lipopolysaccharide insertion. Nature. 2014 Jul 3;511(7507):52-6. doi: 10.1038/nature13464. Epub 2014 Jun 18. PMID:24990744 doi:http://dx.doi.org/10.1038/nature13464
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