1ytr
From Proteopedia
(New page: 200px<br /><applet load="1ytr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ytr" /> '''NMR structure of plantaricin a in dpc micell...) |
|||
| Line 1: | Line 1: | ||
| - | [[Image:1ytr.gif|left|200px]]<br /><applet load="1ytr" size=" | + | [[Image:1ytr.gif|left|200px]]<br /><applet load="1ytr" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1ytr" /> | caption="1ytr" /> | ||
'''NMR structure of plantaricin a in dpc micelles, 20 structures'''<br /> | '''NMR structure of plantaricin a in dpc micelles, 20 structures'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The three-dimensional structure in dodecyl phosphocholine micelles of the | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1YTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http:// | + | 1YTR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1YTR OCA]. |
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fimland, G.]] | [[Category: Fimland, G.]] | ||
| - | [[Category: Kristiansen, P | + | [[Category: Kristiansen, P E.]] |
[[Category: Mantzilas, D.]] | [[Category: Mantzilas, D.]] | ||
[[Category: Nissen-Meyer, J.]] | [[Category: Nissen-Meyer, J.]] | ||
| Line 21: | Line 21: | ||
[[Category: pheromone]] | [[Category: pheromone]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:09:00 2008'' |
Revision as of 14:09, 21 February 2008
|
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.
About this Structure
1YTR is a Single protein structure of sequence from [1]. Full crystallographic 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 Thu Feb 21 16:09:00 2008
