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| - | ==SOLUTION STRUCTURE OF BACTERIOCIN AS-48== | + | |
| - | <StructureSection load='1e68' size='340' side='right' caption='[[1e68]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | ==Solution structure of bacteriocin AS-48== |
| | + | <StructureSection load='1e68' size='340' side='right'caption='[[1e68]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1e68]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1E68 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1e68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Enterococcus_faecalis Enterococcus faecalis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E68 FirstGlance]. <br> |
| - | </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=1e68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e68 OCA], [http://pdbe.org/1e68 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1e68 RCSB], [http://www.ebi.ac.uk/pdbsum/1e68 PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1e68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e68 OCA], [https://pdbe.org/1e68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e68 RCSB], [https://www.ebi.ac.uk/pdbsum/1e68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e68 ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/Q47765_ENTFL Q47765_ENTFL] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Enterococcus faecalis]] | | [[Category: Enterococcus faecalis]] |
| - | [[Category: Bruix, M]] | + | [[Category: Large Structures]] |
| - | [[Category: Galvez, A]] | + | [[Category: Bruix M]] |
| - | [[Category: Gonzalez, C]] | + | [[Category: Galvez A]] |
| - | [[Category: Langdon, G]] | + | [[Category: Gonzalez C]] |
| - | [[Category: Maqueda, M]] | + | [[Category: Langdon G]] |
| - | [[Category: Rico, M]] | + | [[Category: Maqueda M]] |
| - | [[Category: Valdivia, E]] | + | [[Category: Rico M]] |
| - | [[Category: Antibiotic]]
| + | [[Category: Valdivia E]] |
| - | [[Category: Bacteriocin]]
| + | |
| - | [[Category: Cationic antibacterial peptide]]
| + | |
| - | [[Category: Cyclic polypeptide]]
| + | |
| - | [[Category: Five-helix globule]]
| + | |
| Structural highlights
Function
Q47765_ENTFL
Publication Abstract from PubMed
The solution structure of bacteriocin AS-48, a 70-residue cyclic polypeptide from Enterococcus faecalis, consists of a globular arrangement of five alpha-helices enclosing a compact hydrophobic core. The head-to-tail union lies in the middle of helix 5, a fact that is shown to have a pronounced effect on the stability of the three-dimensional structure. Positive charges in the side chains of residues in helix 4 and in the turn linking helix 4 to helix 5 form a cluster that most probably determine its antibacterial activity by promoting pore formation in cell membranes. A similar five-helix structural motif has been found in the antimicrobial NK-lysin, an effector polypeptide of T and natural killer (NK) cells. Bacteriocin AS-48 lacks the three disulfide bridges characteristic of the saposin fold present in NK-lysin, and has no sequence homology with it. Nevertheless, the similar molecular architecture and high positive charge strongly suggest a common mechanism of antibacterial action.
Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin.,Gonzalez C, Langdon GM, Bruix M, Galvez A, Valdivia E, Maqueda M, Rico M Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6. PMID:11005847[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Gonzalez C, Langdon GM, Bruix M, Galvez A, Valdivia E, Maqueda M, Rico M. Bacteriocin AS-48, a microbial cyclic polypeptide structurally and functionally related to mammalian NK-lysin. Proc Natl Acad Sci U S A. 2000 Oct 10;97(21):11221-6. PMID:11005847 doi:10.1073/pnas.210301097
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