View source for 1og7


==Three-dimensional structure in lipid micelles of the pediocin-like antimicrobial peptide sakacin P.==
<StructureSection load='1og7' size='340' side='right'caption='[[1og7]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1og7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Latilactobacillus_sakei Latilactobacillus sakei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OG7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1OG7 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=1og7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1og7 OCA], [https://pdbe.org/1og7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1og7 RCSB], [https://www.ebi.ac.uk/pdbsum/1og7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1og7 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SAKP_LATSK SAKP_LATSK] Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/og/1og7_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1og7 ConSurf].
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== Publication Abstract from PubMed ==
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.

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<ref>PMID:14516192</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Latilactobacillus sakei]]
[[Category: Fimland G]]
[[Category: Hauge HH]]
[[Category: Mantzilas D]]
[[Category: Markwick PR]]
[[Category: Muhle-Goll C]]
[[Category: Nissen-Meyer J]]
[[Category: Uteng M]]