2a2b: Difference between revisions
New page: left|200px<br /><applet load="2a2b" size="450" color="white" frame="true" align="right" spinBox="true" caption="2a2b" /> '''Curvacin A'''<br /> ==Overview== The 3D str... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2a2b.gif|left|200px]]<br /><applet load="2a2b" size=" | [[Image:2a2b.gif|left|200px]]<br /><applet load="2a2b" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2a2b" /> | caption="2a2b" /> | ||
'''Curvacin A'''<br /> | '''Curvacin A'''<br /> | ||
==Overview== | ==Overview== | ||
The 3D structure of the membrane-permeabilizing 41-mer pediocin-like | The 3D structure of the membrane-permeabilizing 41-mer pediocin-like antimicrobial peptide curvacin A produced by lactic acid bacteria has been studied by NMR spectroscopy. In DPC micelles, the cationic and hydrophilic N-terminal half of the peptide forms an S-shaped beta-sheet-like domain stabilized by a disulfide bridge and a few hydrogen bonds. This domain is followed by two alpha-helices: a hydrophilic 6-mer helix between residues 19 and 24 and an amphiphilic/hydrophobic 11-mer helix between residues 29 and 39. There are two hinges in the peptide, one at residues 16-18 between the N-terminal S-shaped beta-sheet-like structure and the central 6-mer helix and one at residues 26-28 between the central helix and the 11-mer C-terminal helix. The latter helix is the only amphiphilic/hydrophobic part of the peptide and is thus presumably the part that penetrates into the hydrophobic phase of target-cell membranes. The hinge between the two helices may introduce the flexibility that allows the helix to dip into membranes. The helix-hinge-helix structure in the C-terminal half of curvacin A clearly distinguishes this peptide from the other pediocin-like peptides whose structures have been analyzed and suggests that curvacin A along with the structural homologues enterocin P and carnobacteriocin BM1 belong to a subgroup of the pediocin-like family of antimicrobial peptides. | ||
==About this Structure== | ==About this Structure== | ||
2A2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_curvatus Lactobacillus curvatus]. Full crystallographic information is available from [http:// | 2A2B is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_curvatus Lactobacillus curvatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2B OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Lactobacillus curvatus]] | [[Category: Lactobacillus curvatus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Haugen, H | [[Category: Haugen, H S.]] | ||
[[Category: Kristiansen, P | [[Category: Kristiansen, P E.]] | ||
[[Category: alfa helix]] | [[Category: alfa helix]] | ||
[[Category: beta-sheet like strukture]] | [[Category: beta-sheet like strukture]] | ||
[[Category: peptide]] | [[Category: peptide]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:22:55 2008'' | ||
Revision as of 17:22, 21 February 2008
|
Curvacin A
OverviewOverview
The 3D structure of the membrane-permeabilizing 41-mer pediocin-like antimicrobial peptide curvacin A produced by lactic acid bacteria has been studied by NMR spectroscopy. In DPC micelles, the cationic and hydrophilic N-terminal half of the peptide forms an S-shaped beta-sheet-like domain stabilized by a disulfide bridge and a few hydrogen bonds. This domain is followed by two alpha-helices: a hydrophilic 6-mer helix between residues 19 and 24 and an amphiphilic/hydrophobic 11-mer helix between residues 29 and 39. There are two hinges in the peptide, one at residues 16-18 between the N-terminal S-shaped beta-sheet-like structure and the central 6-mer helix and one at residues 26-28 between the central helix and the 11-mer C-terminal helix. The latter helix is the only amphiphilic/hydrophobic part of the peptide and is thus presumably the part that penetrates into the hydrophobic phase of target-cell membranes. The hinge between the two helices may introduce the flexibility that allows the helix to dip into membranes. The helix-hinge-helix structure in the C-terminal half of curvacin A clearly distinguishes this peptide from the other pediocin-like peptides whose structures have been analyzed and suggests that curvacin A along with the structural homologues enterocin P and carnobacteriocin BM1 belong to a subgroup of the pediocin-like family of antimicrobial peptides.
About this StructureAbout this Structure
2A2B is a Single protein structure of sequence from Lactobacillus curvatus. Full crystallographic information is available from OCA.
ReferenceReference
Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide curvacin A., Haugen HS, Fimland G, Nissen-Meyer J, Kristiansen PE, Biochemistry. 2005 Dec 13;44(49):16149-57. PMID:16331975
Page seeded by OCA on Thu Feb 21 16:22:55 2008