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| | ==NMR structure of microplusin a antimicrobial peptide from Rhipicephalus (Boophilus) microplus== | | ==NMR structure of microplusin a antimicrobial peptide from Rhipicephalus (Boophilus) microplus== |
| - | <StructureSection load='2knj' size='340' side='right'caption='[[2knj]], [[NMR_Ensembles_of_Models | 15 NMR models]]' scene=''> | + | <StructureSection load='2knj' size='340' side='right'caption='[[2knj]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2knj]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Boophilus_microplus Boophilus microplus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KNJ OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2KNJ FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2knj]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rhipicephalus_microplus Rhipicephalus microplus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2KNJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2KNJ FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2knj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knj OCA], [http://pdbe.org/2knj PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2knj RCSB], [http://www.ebi.ac.uk/pdbsum/2knj PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2knj ProSAT]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 15 models</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=2knj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2knj OCA], [https://pdbe.org/2knj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2knj RCSB], [https://www.ebi.ac.uk/pdbsum/2knj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2knj ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/MPSIN_RHIMP MPSIN_RHIMP]] Has bacteriostatic activity against the Gram-positive bacterium M.luteus, but not against Gram-negative bacterium E.coli SBS363. Has fungistatic activity against C.neoformans, but not C.albicans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus.<ref>PMID:14642886</ref> | + | [https://www.uniprot.org/uniprot/MPSIN_RHIMP MPSIN_RHIMP] Has bacteriostatic activity against the Gram-positive bacterium M.luteus, but not against Gram-negative bacterium E.coli SBS363. Has fungistatic activity against C.neoformans, but not C.albicans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus.<ref>PMID:14642886</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | <jmolCheckbox> | | <jmolCheckbox> |
| | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/2knj_consurf.spt"</scriptWhenChecked> | | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/kn/2knj_consurf.spt"</scriptWhenChecked> |
| - | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | + | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> |
| | <text>to colour the structure by Evolutionary Conservation</text> | | <text>to colour the structure by Evolutionary Conservation</text> |
| | </jmolCheckbox> | | </jmolCheckbox> |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Boophilus microplus]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Daffre, S]] | + | [[Category: Rhipicephalus microplus]] |
| - | [[Category: Pires, J R]] | + | [[Category: Daffre S]] |
| - | [[Category: Rezende, C A]] | + | [[Category: Pires JR]] |
| - | [[Category: Silva, F D]] | + | [[Category: Rezende CA]] |
| - | [[Category: Antimicrobial peptide]] | + | [[Category: Silva FD]] |
| - | [[Category: Antimicrobial protein]]
| + | |
| - | [[Category: Microplusin]]
| + | |
| Structural highlights
Function
MPSIN_RHIMP Has bacteriostatic activity against the Gram-positive bacterium M.luteus, but not against Gram-negative bacterium E.coli SBS363. Has fungistatic activity against C.neoformans, but not C.albicans. Binds and sequesters copper and iron ions. Copper-chelating is crucial for antimicrobial activity against M.luteus.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Microplusin, a Rhipicephalus (Boophilus) microplus antimicrobial peptide (AMP) is the first fully characterized member of a new family of cysteine-rich AMPs with histidine-rich regions at the N and C termini. In the tick, microplusin belongs to the arsenal of innate defense molecules active against bacteria and fungi. Here we describe the NMR solution structure of microplusin and demonstrate that the protein binds copper II and iron II. Structured as a single alpha-helical globular domain, microplusin consists of five alpha-helices: alpha1 (residues Gly-9 to Arg-21), alpha2 (residues Glu-27 to Asn-40), alpha3 (residues Arg-44 to Thr-54), alpha4 (residues Leu-57 to Tyr-64), and alpha5 (residues Asn-67 to Cys-80). The N and C termini are disordered. This structure is unlike any other AMP structures described to date. We also used NMR spectroscopy to map the copper binding region on microplusin. Finally, using the Gram-positive bacteria Micrococcus luteus as a model, we studied of mode of action of microplusin. Microplusin has a bacteriostatic effect and does not permeabilize the bacterial membrane. Because microplusin binds metals, we tested whether this was related to its antimicrobial activity. We found that the bacteriostatic effect of microplusin was fully reversed by supplementation of culture media with copper II but not iron II. We also demonstrated that microplusin affects M. luteus respiration, a copper-dependent process. Thus, we conclude that the antibacterial effect of microplusin is due to its ability to bind and sequester copper II.
Structure and mode of action of microplusin, a copper II-chelating antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus) microplus.,Silva FD, Rezende CA, Rossi DC, Esteves E, Dyszy FH, Schreier S, Gueiros-Filho F, Campos CB, Pires JR, Daffre S J Biol Chem. 2009 Dec 11;284(50):34735-46. Epub 2009 Oct 14. PMID:19828445[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fogaca AC, Lorenzini DM, Kaku LM, Esteves E, Bulet P, Daffre S. Cysteine-rich antimicrobial peptides of the cattle tick Boophilus microplus: isolation, structural characterization and tissue expression profile. Dev Comp Immunol. 2004 Mar;28(3):191-200. PMID:14642886
- ↑ Silva FD, Rezende CA, Rossi DC, Esteves E, Dyszy FH, Schreier S, Gueiros-Filho F, Campos CB, Pires JR, Daffre S. Structure and mode of action of microplusin, a copper II-chelating antimicrobial peptide from the cattle tick Rhipicephalus (Boophilus) microplus. J Biol Chem. 2009 Dec 11;284(50):34735-46. Epub 2009 Oct 14. PMID:19828445 doi:10.1074/jbc.M109.016410
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