1og7

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{{STRUCTURE_1og7| PDB=1og7 | SCENE= }}
{{STRUCTURE_1og7| PDB=1og7 | SCENE= }}
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'''THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.'''
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===THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.===
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==Overview==
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The three-dimensional structures in dodecylphosphocholine (DPC) micelles and in trifluoroethanol (TFE) of the pediocin-like antimicrobial peptide sakacin P and an engineered variant of sakacin P (termed sakP[N24C+44C]) have been determined by use of nuclear magnetic resonance spectroscopy. SakP[N24C+44C] has an inserted non-native activity- and structure-stabilizing C-terminal disulfide bridge that ties the C-terminus to the middle part of the peptide. In the presence of DPC, the cationic N-terminal region (residues 1-17) of both peptides has an S-shaped conformation that is reminiscent of a three-stranded antiparallel beta-sheet and that is more pronounced when the peptide was dissolved in TFE instead of DPC. The four positively charged residues located in the N-terminal part are found pointing to the same direction. For both peptides, the N-terminal region is followed by a well-defined central amphiphilic alpha-helix (residues 18-33), and this in turn is followed by the C-terminal tail (residues 34-43 for sakacin P and 34-44 for sakP[N24C+44C]) that lacks any apparent common secondary structural motif. In the presence of DPC, the C-terminal tails in both peptides fold back onto the central alpha-helix, thereby creating a hairpin-like structure in the C-terminal halves. The lack of long-range NOEs between the beta-sheet Nu-terminal region and the hairpin-like C-terminal half indicates that there is a flexible hinge between these regions. We discuss which implications such a structural arrangement has on the interaction with the target cell membrane.
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(as it appears on PubMed at http://www.pubmed.gov), where 14516192 is the PubMed ID number.
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{{ABSTRACT_PUBMED_14516192}}
==About this Structure==
==About this Structure==
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1OG7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_sakei Lactobacillus sakei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG7 OCA].
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1OG7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_sakei Lactobacillus sakei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG7 OCA].
==Reference==
==Reference==
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[[Category: Pediocin-like bacteriocin]]
[[Category: Pediocin-like bacteriocin]]
[[Category: Sakacin p]]
[[Category: Sakacin p]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 03:48:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 08:46:24 2008''

Revision as of 05:46, 29 July 2008

Image:1og7.png

Template:STRUCTURE 1og7

THREE-DIMENSIONAL STRUCTURE IN LIPID MICELLES OF THE PEDIOCIN-LIKE ANTIMICROBIAL PEPTIDE SAKACIN P.

Template:ABSTRACT PUBMED 14516192

About this Structure

1OG7 is a Single protein structure of sequence from Lactobacillus sakei. Full experimental information is available from OCA.

Reference

Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P and a sakacin P variant that is structurally stabilized by an inserted C-terminal disulfide bridge., Uteng M, Hauge HH, Markwick PR, Fimland G, Mantzilas D, Nissen-Meyer J, Muhle-Goll C, Biochemistry. 2003 Oct 7;42(39):11417-26. PMID:14516192

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