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2mhw

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==The solution NMR structure of maximin-4 in SDS micelles==
==The solution NMR structure of maximin-4 in SDS micelles==
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<StructureSection load='2mhw' size='340' side='right' caption='[[2mhw]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2mhw' size='340' side='right'caption='[[2mhw]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2mhw]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MHW FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2mhw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bombina_maxima Bombina maxima]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MHW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MHW FirstGlance]. <br>
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</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhw OCA], [http://pdbe.org/2mhw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mhw RCSB], [http://www.ebi.ac.uk/pdbsum/2mhw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhw ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=2mhw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mhw OCA], [https://pdbe.org/2mhw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mhw RCSB], [https://www.ebi.ac.uk/pdbsum/2mhw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mhw ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/M4H33_BOMMX M4H33_BOMMX] Maximin-4 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans, but not against A.flavus nor P.uticale. It has little hemolytic activity. It does not possess a significant cytotoxicity against tumor cell lines. It does not possess a significant anti-HIV activity. Maximin-H3 shows antibacterial activity against both Gram-positive and Gram-negative bacteria. It shows also antimicrobial activity against the fungus C.albicans. Shows strong hemolytic activity.
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Maximin-4 is a 27-residue cationic antimicrobial peptide exhibiting selectivity for bacterial cells. As part of the innate defense system in the Chinese red-belly toad, its mode of action is thought to be ion channel or pore formation and dissipation of the electrochemical gradient across the pathogenic cell membrane. Here we present the high-resolution structure of maximin-4 in two different membrane mimetics, sodium dodecyl sulfate micelles and 50% methanol, as determined by (1)H solution NMR spectroscopy. In both environments, the peptide chain adopts a helix-break-helix conformation following a highly disordered N-terminal segment. Despite the similarities in the overall topology of the two structures, major differences are observed in terms of the interactions stabilizing the kink region and the arrangement of the four lysine residues. This has a marked influence on the shape and charge distribution of the molecule and may have implications for the bacterial selectivity of the peptide. The solution NMR results are complemented by CD spectroscopy and solid-state NMR experiments in lipid bilayers, both confirming the predominantly helical conformation of the peptide. As a first step in elucidating the membrane interactions of maximin-4, our study contributes to a better understanding of the mode of action of antimicrobial peptides and the factors governing their selectivity.
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A kinked antimicrobial peptide from Bombina maxima. I. Three-dimensional structure determined by NMR in membrane-mimicking environments.,Toke O, Banoczi Z, Kiraly P, Heinzmann R, Burck J, Ulrich AS, Hudecz F Eur Biophys J. 2011 Apr;40(4):447-62. doi: 10.1007/s00249-010-0657-0. Epub 2011, Jan 14. PMID:21234559<ref>PMID:21234559</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2mhw" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Banoczi, Z]]
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[[Category: Bombina maxima]]
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[[Category: Burck, J]]
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[[Category: Large Structures]]
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[[Category: Heinzmann, R]]
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[[Category: Banoczi Z]]
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[[Category: Hudecz, F]]
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[[Category: Burck J]]
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[[Category: Kiraly, P]]
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[[Category: Heinzmann R]]
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[[Category: Toke, O]]
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[[Category: Hudecz F]]
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[[Category: Ulrich, A S]]
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[[Category: Kiraly P]]
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[[Category: Antimicrobial peptide]]
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[[Category: Toke O]]
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[[Category: Antimicrobial protein]]
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[[Category: Ulrich AS]]
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[[Category: Bacterial resistance]]
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[[Category: Lipid bilayer]]
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[[Category: Membrane peptide]]
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[[Category: Membrane protein]]
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Current revision

The solution NMR structure of maximin-4 in SDS micelles

PDB ID 2mhw

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