2mw6

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==Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue==
==Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue==
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<StructureSection load='2mw6' size='340' side='right'caption='[[2mw6]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
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<StructureSection load='2mw6' size='340' side='right'caption='[[2mw6]]' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2mw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MW6 FirstGlance]. <br>
<table><tr><td colspan='2'>[[2mw6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Apis_mellifera Apis mellifera]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MW6 FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3UQ:[(1,2,3,4,5-ETA)-CYCLOPENTADIENYL][(1,2,3,4,4A,8A-ETA)-NAPHTHALENE]RUTHENIUM(1+)'>3UQ</scene></td></tr>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3UQ:[(1,2,3,4,5-ETA)-CYCLOPENTADIENYL][(1,2,3,4,4A,8A-ETA)-NAPHTHALENE]RUTHENIUM(1+)'>3UQ</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></td></tr>
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<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2mlt|2mlt]]</div></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=2mw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw6 OCA], [https://pdbe.org/2mw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mw6 RCSB], [https://www.ebi.ac.uk/pdbsum/2mw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw6 ProSAT]</span></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=2mw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mw6 OCA], [https://pdbe.org/2mw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mw6 RCSB], [https://www.ebi.ac.uk/pdbsum/2mw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mw6 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME]] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
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[https://www.uniprot.org/uniprot/MEL_APIME MEL_APIME] Melittin: Main toxin of bee venom with strong hemolytic activity. Forms a pore in the cell membrane by inserting into lipid bilayers in an alpha-helical conformation and has multiple effects, probably, as a result of its interaction with negatively charged phospholipids. It inhibits well known transport pumps such as the Na(+)-K(+)-ATPase and the H(+)-K(+)-ATPase. It increases the permeability of cell membranes to ions, particularly Na(+) and indirectly Ca(2+), because of the Na(+)-Ca(2+)-exchange. It acts synergistically with phospholipase A2.<ref>PMID:20472009</ref> Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.<ref>PMID:20472009</ref>
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== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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[[Category: Apis mellifera]]
[[Category: Apis mellifera]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Novikov, V V]]
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[[Category: Novikov VV]]
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[[Category: Pavlov, A A]]
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[[Category: Pavlov AA]]
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[[Category: Perekalin, D S]]
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[[Category: Perekalin DS]]
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[[Category: Toxin]]
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Revision as of 09:48, 14 June 2023

Structure of the bee venom toxin melittin with [(C5H5)Ru]+ fragment attached to the tryptophan residue

PDB ID 2mw6

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