1og7

<StructureSection load='1og7' size='340' side='right'caption='[[1og7]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1og7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_15521 Atcc 15521]. 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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ohm|1ohm]], [[1ohn|1ohn]]</div></td></tr>

[[https://www.uniprot.org/uniprot/SAKP_LACSK SAKP_LACSK]] Bactericidal activity; inhibits closely related Lactobacilli, Listeria monocytogenes and ivanovvi, Enterococcus faecalis, Carnobacterium sp and Brocothrix thermosphacta.

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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/>

[[Category: Atcc 15521]]

[[Category: Fimland, G]]

[[Category: Hauge, H H]]

[[Category: Mantzilas, D]]

[[Category: Markwick, P R]]

[[Category: Muhle-Goll, C]]

[[Category: Nissen-Meyer, J]]

[[Category: Uteng, M]]

[[Category: Sakacin p]]