1wco

From Proteopedia

(Difference between revisions)

Revision as of 04:36, 10 September 2015

The solution structure of the nisin-lipid II complex

Structural highlights

1wco is a 2 chain structure with sequence from Lactococcus lactis and Monarthropalpus flavus. This structure supersedes the now removed PDB entry 1uzt. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
NonStd Res:	, , , , ,
Related:	1aj1, 1mqx, 1mqy, 1mqz, 1qow, 1w9n, 2dde, 2ktn, 2kto
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[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.

Publication Abstract from PubMed

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.

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^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Hsu ST, Breukink E, Tischenko E, Lutters MA, de Kruijff B, Kaptein R, Bonvin AM, van Nuland NA. The nisin-lipid II complex reveals a pyrophosphate cage that provides a blueprint for novel antibiotics. Nat Struct Mol Biol. 2004 Oct;11(10):963-7. Epub 2004 Sep 12. PMID:15361862 doi:10.1038/nsmb830

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1wco"

@@ Line 6: / Line 6: @@
 <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><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=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene>, <scene name='pdbligand=MUB:N-ACETYLMURAMIC+ACID'>MUB</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aj1|1aj1]], [[1mqx|1mqx]], [[1mqy|1mqy]], [[1mqz|1mqz]], [[1qow|1qow]], [[1w9n|1w9n]], [[2dde|2dde]], [[2ktn|2ktn]], [[2kto|2kto]]</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=1wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wco OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1wco RCSB], [http://www.ebi.ac.uk/pdbsum/1wco PDBsum]</span></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=1wco FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1wco OCA], [http://pdbe.org/1wco PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1wco RCSB], [http://www.ebi.ac.uk/pdbsum/1wco PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/LANZ_LACLA LANZ_LACLA]] 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.
+[[http://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.
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 18: / Line 18: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1wco" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>

1wco

From Proteopedia

Revision as of 04:36, 10 September 2015

The solution structure of the nisin-lipid II complex

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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