6gd5
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | The | + | ==The solution structure of the LptA-Thanatin complex== |
| + | <StructureSection load='6gd5' size='340' side='right'caption='[[6gd5]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6gd5]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Podisus_maculiventris Podisus maculiventris]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6GD5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6GD5 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</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=6gd5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6gd5 OCA], [https://pdbe.org/6gd5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6gd5 RCSB], [https://www.ebi.ac.uk/pdbsum/6gd5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6gd5 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/LPTA_ECOLI LPTA_ECOLI] Involved in the assembly of lipopolysaccharide (LPS). Required for the translocation of LPS from the inner membrane to the outer membrane. May form a bridge between the inner membrane and the outer membrane, via interactions with LptC and LptD, thereby facilitating LPS transfer across the periplasm.[HAMAP-Rule:MF_01914]<ref>PMID:16765569</ref> <ref>PMID:17056748</ref> <ref>PMID:18424520</ref> <ref>PMID:18480051</ref> <ref>PMID:21169485</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | With the increasing resistance of many Gram-negative bacteria to existing classes of antibiotics, identifying new paradigms in antimicrobial discovery is an important research priority. Of special interest are the proteins required for the biogenesis of the asymmetric Gram-negative bacterial outer membrane (OM). Seven Lpt proteins (LptA to LptG) associate in most Gram-negative bacteria to form a macromolecular complex spanning the entire envelope, which transports lipopolysaccharide (LPS) molecules from their site of assembly at the inner membrane to the cell surface, powered by adenosine 5'-triphosphate hydrolysis in the cytoplasm. The periplasmic protein LptA comprises the protein bridge across the periplasm, which connects LptB2FGC at the inner membrane to LptD/E anchored in the OM. We show here that the naturally occurring, insect-derived antimicrobial peptide thanatin targets LptA and LptD in the network of periplasmic protein-protein interactions required to assemble the Lpt complex, leading to the inhibition of LPS transport and OM biogenesis in Escherichia coli. | ||
| - | + | Thanatin targets the intermembrane protein complex required for lipopolysaccharide transport in Escherichia coli.,Vetterli SU, Zerbe K, Muller M, Urfer M, Mondal M, Wang SY, Moehle K, Zerbe O, Vitale A, Pessi G, Eberl L, Wollscheid B, Robinson JA Sci Adv. 2018 Nov 14;4(11):eaau2634. doi: 10.1126/sciadv.aau2634. eCollection, 2018 Nov. PMID:30443594<ref>PMID:30443594</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6gd5" style="background-color:#fffaf0;"></div> |
| - | [[Category: Moehle | + | == References == |
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Escherichia coli K-12]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Podisus maculiventris]] | ||
| + | [[Category: Moehle K]] | ||
| + | [[Category: Zerbe O]] | ||
Current revision
The solution structure of the LptA-Thanatin complex
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