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6dst

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Recombinant melittin

Structural highlights

6dst is a 1 chain structure with sequence from Apis mellifera. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

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.^[1] Melittin-S: 1.4-fold less hemolytic and adopts a less organized secondary structure than melittin.^[2]

Publication Abstract from PubMed

Melittin is an extensively studied, 26-residue toxic peptide from honey-bee venom. Because of its versatility in adopting a variety of secondary (helix or coil), and quaternary (monomer or tetramer) structures in various environments, melittin has been the focus of numerous investigations as a model peptide in protein folding studies, as well as in studies involving binding to proteins, lipids and polysaccharides. A significant body of evidence supports the view that melittin binds to these macromolecules in a predominantly helical conformation, but detailed structural knowledge of this conformation is lacking. In this report, we present nuclear magnetic resonance (NMR)-based structural insights into the helix formation of recombinant melittin in the presence of TFE - a known secondary structure inducer in peptides. These studies were performed at neutral pH, with micromolar amounts of the peptide. Using Nuclear Overhauser effect (NOE)-derived distance restraints from 3D NMR spectra, we determined the atomic resolution NMR solution structure of recombinant melittin bearing a TFE-stabilized helix. To circumvent the complications with structure determination of small peptides with high conformational flexibility, we developed a workflow for enhancing proton NOEs by increasing the viscosity of the medium. In the TFE-containing medium, recombinant monomeric melittin forms a long, continuous helical structure, which consists of the N-and C-terminal alpha-helices and the non-canonical 310-helix in the middle. The non-canonical 310-helix is missing in the previously solved X-ray structure of tetrameric melittin and the NMR structure of melittin in methanol. Melittin's structure in TFE containing medium provides insights into melittin's conformational transitions, which are relevant to the peptide's interactions with its biological targets.

Helical Structure of Recombinant Melittin.,Ramirez LS, Pande J, Shekhtman A J Phys Chem B. 2018 Dec 20. doi: 10.1021/acs.jpcb.8b08424. PMID:30570258^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
↑ Sciani JM, Marques-Porto R, Lourenco Junior A, Orsi Rde O, Ferreira Junior RS, Barraviera B, Pimenta DC. Identification of a novel melittin isoform from Africanized Apis mellifera venom. Peptides. 2010 Aug;31(8):1473-9. doi: 10.1016/j.peptides.2010.05.001. Epub 2010, May 21. PMID:20472009 doi:http://dx.doi.org/10.1016/j.peptides.2010.05.001
↑ Ramirez LS, Pande J, Shekhtman A. Helical Structure of Recombinant Melittin. J Phys Chem B. 2018 Dec 20. doi: 10.1021/acs.jpcb.8b08424. PMID:30570258 doi:http://dx.doi.org/10.1021/acs.jpcb.8b08424

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/6dst"

Categories: Apis mellifera | Large Structures | Pande J | Ramirez LM | Shekhtman A

@@ Line 1: / Line 1: @@
 ==Recombinant melittin==
-<StructureSection load='6dst' size='340' side='right'caption='[[6dst]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='6dst' size='340' side='right'caption='[[6dst]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6dst]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DST OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DST FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6dst]] 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=6DST OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6DST FirstGlance]. <br>
-</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=6dst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dst OCA], [http://pdbe.org/6dst PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dst RCSB], [http://www.ebi.ac.uk/pdbsum/6dst PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dst ProSAT]</span></td></tr>
+</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=6dst FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dst OCA], [https://pdbe.org/6dst PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6dst RCSB], [https://www.ebi.ac.uk/pdbsum/6dst PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6dst ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://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>
+[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>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 21: / Line 21: @@
 __TOC__
 </StructureSection>
+[[Category: Apis mellifera]]
 [[Category: Large Structures]]
-[[Category: Pande, J]]
+[[Category: Pande J]]
-[[Category: Ramirez, L M]]
+[[Category: Ramirez LM]]
-[[Category: Shekhtman, A]]
+[[Category: Shekhtman A]]
-[[Category: Alpha-helical peptide]]
-[[Category: Antibacterial]]
-[[Category: Bee venom]]
-[[Category: Hemolytic]]
-[[Category: Toxin]]

6dst

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Current revision

Recombinant melittin

Structural highlights

Function

Publication Abstract from PubMed

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