From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1ytr.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1ytr.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1ytr| PDB=1ytr | SCENE= }} | | {{STRUCTURE_1ytr| PDB=1ytr | SCENE= }} |
| | | | |
| - | '''NMR structure of plantaricin a in dpc micelles, 20 structures'''
| + | ===NMR structure of plantaricin a in dpc micelles, 20 structures=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | The three-dimensional structure in dodecyl phosphocholine micelles of the 26-mer membrane-permeabilizing bacteriocin-like pheromone plantaricin A (PlnA) has been determined by use of nuclear magnetic resonance spectroscopy. The peptide was unstructured in water but became partly structured upon exposure to micelles. An amphiphilic alpha-helix stretching from residue 12 to 21 (possibly also including residues 22 and 23) was then formed in the C-terminal part of the peptide, whereas the N-terminal part remained largely unstructured. PlnA exerted its membrane-permeabilizing antimicrobial activity through a nonchiral interaction with the target cell membrane because the d-enantiomeric form had the same activity as the natural l-form. This nonchiral interaction involved the amphiphilic alpha-helical region in the C-terminal half of PlnA because a 17-mer fragment that contains the amphiphilic alpha-helical part of the peptide had antimicrobial potency that was similar to that of the l- and d-enantiomeric forms of PlnA. Also the pheromone activity of PlnA depended on this nonchiral interaction because both the l- and d-enantiomeric forms of the 17-mer fragment inhibited the pheromone activity. The pheromone activity also involved, however, a chiral interaction between the N-terminal part of PlnA and its receptor because high concentrations of the l-form (but not the d-form) of a 5-mer fragment derived from the N-terminal part of PlnA had pheromone activity. The results thus reveal a novel mechanism whereby peptide pheromones such as PlnA may function. An initial nonchiral interaction with membrane lipids induces alpha-helical structuring in a segment of the peptide pheromone. The peptide becomes thereby sufficiently structured and properly positioned in the membrane interface, thus enabling it to engage in a chiral interaction with its receptor in or near the membrane water interface. This membrane-interacting mode of action explains why some peptide pheromones/hormones such as PlnA sometimes display antimicrobial activity in addition to their pheromone activity.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15805109}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15805109 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15805109}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| - | 1YTR is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTR OCA]. | + | 1YTR is a [[Single protein]] structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTR OCA]. |
| | | | |
| | ==Reference== | | ==Reference== |
| Line 29: |
Line 33: |
| | [[Category: Micelle]] | | [[Category: Micelle]] |
| | [[Category: Pheromone]] | | [[Category: Pheromone]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 16:46:46 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 05:52:39 2008'' |
Revision as of 02:52, 29 July 2008
Template:STRUCTURE 1ytr
NMR structure of plantaricin a in dpc micelles, 20 structures
Template:ABSTRACT PUBMED 15805109
About this Structure
1YTR is a Single protein structure. Full experimental information is available from OCA.
Reference
Structure and mode of action of the membrane-permeabilizing antimicrobial peptide pheromone plantaricin A., Kristiansen PE, Fimland G, Mantzilas D, Nissen-Meyer J, J Biol Chem. 2005 Jun 17;280(24):22945-50. Epub 2005 Apr 1. PMID:15805109
Page seeded by OCA on Tue Jul 29 05:52:39 2008
