2a2b: Difference between revisions

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{{Seed}}
[[Image:2a2b.png|left|200px]]


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==Curvacin A==
The line below this paragraph, containing "STRUCTURE_2a2b", creates the "Structure Box" on the page.
<StructureSection load='2a2b' size='340' side='right'caption='[[2a2b]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2a2b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Latilactobacillus_curvatus Latilactobacillus curvatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2A2B FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2a2b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a2b OCA], [https://pdbe.org/2a2b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2a2b RCSB], [https://www.ebi.ac.uk/pdbsum/2a2b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2a2b ProSAT]</span></td></tr>
{{STRUCTURE_2a2b|  PDB=2a2b  |  SCENE=  }}
</table>
== Function ==
[https://www.uniprot.org/uniprot/SAKA_LATCU SAKA_LATCU] 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/a2/2a2b_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=2a2b ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


===Curvacin A===
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<ref>PMID:16331975</ref>


 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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The line below this paragraph, {{ABSTRACT_PUBMED_16331975}}, adds the Publication Abstract to the page
<div class="pdbe-citations 2a2b" style="background-color:#fffaf0;"></div>
(as it appears on PubMed at http://www.pubmed.gov), where 16331975 is the PubMed ID number.
== References ==
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<references/>
{{ABSTRACT_PUBMED_16331975}}
__TOC__
 
</StructureSection>
==About this Structure==
[[Category: Large Structures]]
2A2B is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Lactobacillus_curvatus Lactobacillus curvatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2A2B OCA].
[[Category: Latilactobacillus curvatus]]
 
[[Category: Haugen HS]]
==Reference==
[[Category: Kristiansen PE]]
<ref group="xtra">PMID:16331975</ref><references group="xtra"/>
[[Category: Lactobacillus curvatus]]
[[Category: Haugen, H S.]]
[[Category: Kristiansen, P E.]]
[[Category: Alfa helix]]
[[Category: Beta-sheet like strukture]]
[[Category: Peptide]]
 
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