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| | <StructureSection load='4q35' size='340' side='right'caption='[[4q35]], [[Resolution|resolution]] 2.39Å' scene=''> | | <StructureSection load='4q35' size='340' side='right'caption='[[4q35]], [[Resolution|resolution]] 2.39Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4q35]] is a 2 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=4Q35 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q35 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4q35]] is a 2 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=4Q35 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Q35 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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]] 2.393Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lptD, imp, ostA, SF0051, S0053 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=623 "Shigella paradysenteriae" Weldin 1927]), lptE, rlpB, SF0640, S0662 ([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=C8E:(HYDROXYETHYLOXY)TRI(ETHYLOXY)OCTANE'>C8E</scene>, <scene name='pdbligand=LDA:LAURYL+DIMETHYLAMINE-N-OXIDE'>LDA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=4q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q35 OCA], [http://pdbe.org/4q35 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4q35 RCSB], [http://www.ebi.ac.uk/pdbsum/4q35 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4q35 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=4q35 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q35 OCA], [https://pdbe.org/4q35 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4q35 RCSB], [https://www.ebi.ac.uk/pdbsum/4q35 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4q35 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/LPTD_SHIFL LPTD_SHIFL]] 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_SHIFL LPTE_SHIFL]] 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_SHIFL LPTD_SHIFL] 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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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Shigella paradysenteriae weldin 1927]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Huang, Y]] | + | [[Category: Shigella flexneri]] |
| - | [[Category: Luo, Q]] | + | [[Category: Huang Y]] |
| - | [[Category: Qiao, S]] | + | [[Category: Luo Q]] |
| - | [[Category: Zhao, Y]] | + | [[Category: Qiao S]] |
| - | [[Category: 26 beita-sheet]]
| + | [[Category: Zhao Y]] |
| - | [[Category: Complex]]
| + | |
| - | [[Category: Lps biogenesis]]
| + | |
| - | [[Category: Membrane protein]]
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| Structural highlights
Function
LPTD_SHIFL Together with LptE, is involved in the assembly of lipopolysaccharide (LPS) at the surface of the outer membrane (By similarity).
Publication Abstract from PubMed
One of the fundamental properties of biological membranes is the asymmetric distribution of membrane lipids. In Gram-negative bacteria, the outer leaflet of the outer membrane is composed predominantly of lipopolysaccharides (LPS). The export of LPS requires seven essential lipopolysaccharide transport (Lpt) proteins to move LPS from the inner membrane, through the periplasm to the surface. Of the seven Lpt proteins, the LptD-LptE complex is responsible for inserting LPS into the external leaflet of the outer membrane. Here we report the crystal structure of the approximately 110-kilodalton membrane protein complex LptD-LptE from Shigella flexneri at 2.4 A resolution. The structure reveals an unprecedented two-protein plug-and-barrel architecture with LptE embedded into a 26-stranded beta-barrel formed by LptD. Importantly, the secondary structures of the first two beta-strands are distorted by two proline residues, weakening their interactions with neighbouring beta-strands and creating a potential portal on the barrel wall that could allow lateral diffusion of LPS into the outer membrane. The crystal structure of the LptD-LptE complex opens the door to new antibiotic strategies targeting the bacterial outer membrane.
Structural basis for lipopolysaccharide insertion in the bacterial outer membrane.,Qiao S, Luo Q, Zhao Y, Zhang XC, Huang Y Nature. 2014 Jul 3;511(7507):108-11. doi: 10.1038/nature13484. Epub 2014 Jun 18. PMID:24990751[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Qiao S, Luo Q, Zhao Y, Zhang XC, Huang Y. Structural basis for lipopolysaccharide insertion in the bacterial outer membrane. Nature. 2014 Jul 3;511(7507):108-11. doi: 10.1038/nature13484. Epub 2014 Jun 18. PMID:24990751 doi:http://dx.doi.org/10.1038/nature13484
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