|
|
| (One intermediate revision not shown.) |
| Line 1: |
Line 1: |
| | | | |
| | ==POLYPHEMUSIN I NMR SOLUTION STRUCTURE== | | ==POLYPHEMUSIN I NMR SOLUTION STRUCTURE== |
| - | <StructureSection load='1rkk' size='340' side='right'caption='[[1rkk]], [[NMR_Ensembles_of_Models | 17 NMR models]]' scene=''> | + | <StructureSection load='1rkk' size='340' side='right'caption='[[1rkk]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1rkk]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKK OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1RKK FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1rkk]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RKK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RKK FirstGlance]. <br> |
| - | </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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'>[http://proteopedia.org/fgij/fg.htm?mol=1rkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rkk OCA], [http://pdbe.org/1rkk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1rkk RCSB], [http://www.ebi.ac.uk/pdbsum/1rkk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1rkk ProSAT]</span></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=1rkk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rkk OCA], [https://pdbe.org/1rkk PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rkk RCSB], [https://www.ebi.ac.uk/pdbsum/1rkk PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rkk ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/PPM1_LIMPO PPM1_LIMPO] Significantly inhibits the growth of Gram-negative and Gram-positive bacteria. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
| Line 21: |
Line 24: |
| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Hancock, R E.W]] | + | [[Category: Synthetic construct]] |
| - | [[Category: Powers, J P.S]] | + | [[Category: Hancock REW]] |
| - | [[Category: Rozek, A]] | + | [[Category: Powers JPS]] |
| - | [[Category: Anti-microbial peptide]] | + | [[Category: Rozek A]] |
| - | [[Category: Antimicrobial peptide]]
| + | |
| - | [[Category: Beta hairpin]]
| + | |
| - | [[Category: Disulfide bridge]]
| + | |
| - | [[Category: Polyphemusin]]
| + | |
| Structural highlights
Function
PPM1_LIMPO Significantly inhibits the growth of Gram-negative and Gram-positive bacteria.
Publication Abstract from PubMed
The solution structure of polyphemusin I was determined using (1)H-NMR spectroscopy. Polyphemusin I was found to be an amphipathic, beta-hairpin connected by a type I' beta-turn. The 17 low-energy structures aligned very well over the beta-sheet region while both termini were poorly defined due in part to a hinge-like region centred in the molecule about arginine residues 6 and 16. Conversely, a linear analogue, PM1-S, with all cysteines simultaneously replaced with serine was found to be dynamic in nature, and a lack of medium and long-range NOEs indicated that this molecule displayed no favoured conformation. Circular dichroism (CD) spectroscopy confirmed that in solution, 50% trifluoroethanol (TFE) and in the presence of liposomes, PM1-S remained unstructured. The antimicrobial activity of PM1-S was found to be 4- to 16-fold less than that of polyphemusin I and corresponded with a 4-fold reduction in bacterial membrane depolarization. Both peptides were able to associate with lipid bilayers in a similar fashion; however, PM1-S was completely unable to translocate model membranes while polyphemusin I retained this activity. It was concluded that the disulfide-constrained, beta-sheet structure of polyphemusin I is required for maximum antimicrobial activity. Disruption of this structure results in reduced antimicrobial activity and completely abolishes membrane translocation indicating that the linear PM1-S acts through a different antimicrobial mechanism.
Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I.,Powers JP, Rozek A, Hancock RE Biochim Biophys Acta. 2004 May 6;1698(2):239-50. PMID:15134657[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Powers JP, Rozek A, Hancock RE. Structure-activity relationships for the beta-hairpin cationic antimicrobial peptide polyphemusin I. Biochim Biophys Acta. 2004 May 6;1698(2):239-50. PMID:15134657 doi:http://dx.doi.org/10.1016/j.bbapap.2003.12.009
|
