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1wco

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==The solution structure of the nisin-lipid II complex==
==The solution structure of the nisin-lipid II complex==
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<StructureSection load='1wco' size='340' side='right' caption='[[1wco]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='1wco' size='340' side='right'caption='[[1wco]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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[[1wco]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] and [http://en.wikipedia.org/wiki/Monarthropalpus_flavus Monarthropalpus flavus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1uzt 1uzt]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCO OCA]. <br>
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<table><tr><td colspan='2'>[[1wco]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis] and [https://en.wikipedia.org/wiki/Monarthropalpus_flavus Monarthropalpus flavus]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1uzt 1uzt]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WCO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1WCO FirstGlance]. <br>
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<b>Related:</b> [[1aj1|1aj1]], [[1mqx|1mqx]], [[1mqy|1mqy]], [[1mqz|1mqz]], [[1qow|1qow]], [[1w9n|1w9n]], [[2dde|2dde]], [[2ktn|2ktn]], [[2kto|2kto]]<br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
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<b>Activity:</b> <span class='plainlinks'>[http://en.wikipedia.org/wiki/Glucokinase Glucokinase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.1.2 2.7.1.2] </span><br>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DAL:D-ALANINE'>DAL</scene>, <scene name='pdbligand=DBB:D-ALPHA-AMINOBUTYRIC+ACID'>DBB</scene>, <scene name='pdbligand=DBU:(2Z)-2-AMINOBUT-2-ENOIC+ACID'>DBU</scene>, <scene name='pdbligand=DHA:2-AMINO-ACRYLIC+ACID'>DHA</scene>, <scene name='pdbligand=FDF:(2E,6E)-12-FLUORO-11-(FLUOROMETHYL)-3,7-DIMETHYLDODECA-2,6,10-TRIEN-1-YL+TRIHYDROGEN+DIPHOSPHATE'>FDF</scene>, <scene name='pdbligand=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene>, <scene name='pdbligand=MUB:N-ACETYLMURAMIC+ACID'>MUB</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
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== Publication Abstract from PubMed ==
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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=1wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wco OCA], [https://pdbe.org/1wco PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1wco RCSB], [https://www.ebi.ac.uk/pdbsum/1wco PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1wco ProSAT]</span></td></tr>
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The emerging antibiotics-resistance problem has underlined the urgent need for novel antimicrobial agents. Lantibiotics (lanthionine-containing antibiotics) are promising candidates to alleviate this problem. Nisin, a member of this family, has a unique pore-forming activity against bacteria. It binds to lipid II, the essential precursor of cell wall synthesis. As a result, the membrane permeabilization activity of nisin is increased by three orders of magnitude. Here we report the solution structure of the complex of nisin and lipid II. The structure shows a novel lipid II-binding motif in which the pyrophosphate moiety of lipid II is primarily coordinated by the N-terminal backbone amides of nisin via intermolecular hydrogen bonds. This cage structure provides a rationale for the conservation of the lanthionine rings among several lipid II-binding lantibiotics. The structure of the pyrophosphate cage offers a template for structure-based design of novel antibiotics.
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</table>
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== Function ==
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The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics.,Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA Nat Struct Mol Biol. 2004 Oct;11(10):963-7. Epub 2004 Sep 12. PMID:15361862<ref>PMID:15361862</ref>
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[https://www.uniprot.org/uniprot/LANZ_LACLL LANZ_LACLL] Lanthionine-containing peptide antibiotic (lantibiotic) active on Gram-positive bacteria. The bactericidal activity of lantibiotics is based on depolarization of energized bacterial cytoplasmic membranes, initiated by the formation of aqueous transmembrane pores.
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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==See Also==
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== References ==
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*[[Nisin|Nisin]]
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lactococcus lactis]]
[[Category: Lactococcus lactis]]
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[[Category: Large Structures]]
[[Category: Monarthropalpus flavus]]
[[Category: Monarthropalpus flavus]]
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[[Category: Bonvin, A M.J J.]]
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[[Category: Bonvin AMJJ]]
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[[Category: Breukink, E.]]
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[[Category: Breukink E]]
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[[Category: Hsu, S T.D.]]
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[[Category: Hsu S-TD]]
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[[Category: Kaptein, R.]]
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[[Category: Kaptein R]]
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[[Category: Kruijff, B De.]]
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[[Category: Lutters MAG]]
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[[Category: Lutters, M A.G.]]
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[[Category: Tischenko E]]
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[[Category: Nuland, N A.J Van.]]
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[[Category: De Kruijff B]]
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[[Category: Tischenko, E.]]
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[[Category: Van Nuland NAJ]]
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[[Category: Antimicrobial]]
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[[Category: Bacteriocin]]
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[[Category: Food preservative]]
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[[Category: Lantibiotic]]
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[[Category: Peptide-antibiotic complex]]
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[[Category: Pore formation]]
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[[Category: Pyrophosphate cage]]
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[[Category: Thioester]]
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Current revision

The solution structure of the nisin-lipid II complex

PDB ID 1wco

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