4nhr

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==Crystal structure of the outer membrane lipopolysaccharide transport protein LptE (RlpB)==
==Crystal structure of the outer membrane lipopolysaccharide transport protein LptE (RlpB)==
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<StructureSection load='4nhr' size='340' side='right' caption='[[4nhr]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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<StructureSection load='4nhr' size='340' side='right'caption='[[4nhr]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[4nhr]] is a 1 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4NHR FirstGlance]. <br>
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<table><tr><td colspan='2'>[[4nhr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4NHR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4NHR FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
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<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=4nhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhr OCA], [http://pdbe.org/4nhr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4nhr RCSB], [http://www.ebi.ac.uk/pdbsum/4nhr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhr ProSAT]</span></td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PEG:DI(HYDROXYETHYL)ETHER'>PEG</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4nhr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4nhr OCA], [https://pdbe.org/4nhr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4nhr RCSB], [https://www.ebi.ac.uk/pdbsum/4nhr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4nhr ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/LPTE_ECOLI LPTE_ECOLI]] 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.<ref>PMID:16861298</ref> <ref>PMID:18424520</ref> <ref>PMID:20203010</ref>
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[https://www.uniprot.org/uniprot/LPTE_ECOLI LPTE_ECOLI] 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.<ref>PMID:16861298</ref> <ref>PMID:18424520</ref> <ref>PMID:20203010</ref>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The assembly of lipopolysaccharide (LPS) on the surface of Gram-negative bacterial cells is essential for their viability and is achieved by the seven-protein LPS transport (Lpt) pathway. The outer membrane (OM) lipoprotein LptE and the beta-barrel membrane protein LptD form a complex that assembles LPS into the outer leaflet of the OM. We report a crystal structure of the Escherichia coli OM lipoprotein LptE at 2.34 A. The structure reveals homology to eukaryotic LPS-binding proteins and allowed for the prediction of an LPS-binding site, which was confirmed by genetic and biophysical experiments. Specific point mutations at this site lead to defects in OM biogenesis. We show that wild-type LptE disrupts LPS-LPS interactions in vitro and that these mutations decrease the ability of LptE to disaggregate LPS. Transmission electron microscopic imaging shows that LptE can disrupt LPS aggregates even at substoichiometric concentrations. We propose a model in which LptE functions as an LPS transfer protein in the OM translocon by disaggregating LPS during transport to allow for its insertion into the OM.
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LptE binds to and alters the physical state of LPS to catalyze its assembly at the cell surface.,Malojcic G, Andres D, Grabowicz M, George AH, Ruiz N, Silhavy TJ, Kahne D Proc Natl Acad Sci U S A. 2014 Jul 1;111(26):9467-72. doi:, 10.1073/pnas.1402746111. Epub 2014 Jun 17. PMID:24938785<ref>PMID:24938785</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 4nhr" style="background-color:#fffaf0;"></div>
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== References ==
== References ==
<references/>
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Kahne, D]]
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[[Category: Escherichia coli K-12]]
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[[Category: Malojcic, G]]
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[[Category: Large Structures]]
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[[Category: 2-layer sandwich]]
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[[Category: Kahne D]]
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[[Category: Gram-negative outer membrane]]
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[[Category: Malojcic G]]
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[[Category: Lipid binding protein]]
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[[Category: Lipopolysaccharide assembly]]
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[[Category: Lysine methylation]]
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Current revision

Crystal structure of the outer membrane lipopolysaccharide transport protein LptE (RlpB)

PDB ID 4nhr

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