This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2k9b
From Proteopedia
(Difference between revisions)
(New page: '''Unreleased structure''' The entry 2k9b is ON HOLD until Oct 07 2010 Authors: Mendonca Moraes, C., Verly, R.M., Resende, J.M., Aisenbrey, C., Bemquerer, M.P., Pilo-Veloso, D., Valente...) |
|||
| (10 intermediate revisions not shown.) | |||
| Line 1: | Line 1: | ||
| - | '''Unreleased structure''' | ||
| - | + | ==Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy== | |
| + | <StructureSection load='2k9b' size='340' side='right'caption='[[2k9b]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[2k9b]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Phyllomedusa_distincta Phyllomedusa distincta]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2K9B OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2K9B FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene></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=2k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2k9b OCA], [https://pdbe.org/2k9b PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2k9b RCSB], [https://www.ebi.ac.uk/pdbsum/2k9b PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2k9b ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/DRS1_PHYDS DRS1_PHYDS] Has antibacterial activity against the Gram-positive bacteria S.aureus and E.faecalis, and the Gram-negative bacteria P.aeruginosa and E.coli. Has antiprotozoal activity against T.cruzi. Has antifungal activity against the yeasts C.tropicalis (MIC=10.1 uM), C.guilliermondii (MIC=20.3 uM), C.albicans (MIC=20.3 uM) and C.albicans ATCC 1023 (MIC=10.1 uM). Decreases viability of murine peritoneal cells. Fuses to, and disrupts liposomes.<ref>PMID:10477123</ref> <ref>PMID:12379643</ref> <ref>PMID:17409003</ref> <ref>PMID:17442605</ref> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | DD K, a peptide first isolated from the skin secretion of the Phyllomedusa distincta frog, has been prepared by solid-phase chemical peptide synthesis and its conformation was studied in trifluoroethanol/water as well as in the presence of sodium dodecyl sulfate and dodecylphosphocholine micelles or small unilamellar vesicles. Multidimensional solution NMR spectroscopy indicates an alpha-helical conformation in membrane environments starting at residue 7 and extending to the C-terminal carboxyamide. Furthermore, DD K has been labeled with (15)N at a single alanine position that is located within the helical core region of the sequence. When reconstituted into oriented phosphatidylcholine membranes the resulting (15)N solid-state NMR spectrum shows a well-defined helix alignment parallel to the membrane surface in excellent agreement with the amphipathic character of DD K. Proton-decoupled (31)P solid-state NMR spectroscopy indicates that the peptide creates a high level of disorder at the level of the phospholipid headgroup suggesting that DD K partitions into the bilayer where it severely disrupts membrane packing. | ||
| - | + | Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy.,Verly RM, de Moraes CM, Resende JM, Aisenbrey C, Bemquerer MP, Pilo-Veloso D, Valente AP, Almeida FC, Bechinger B Biophys J. 2009 Mar 18;96(6):2194-203. PMID:19289046<ref>PMID:19289046</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | <div class="pdbe-citations 2k9b" style="background-color:#fffaf0;"></div> | |
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Phyllomedusa distincta]] | ||
| + | [[Category: Aisenbrey C]] | ||
| + | [[Category: Almeida FCL]] | ||
| + | [[Category: Bechinger B]] | ||
| + | [[Category: Bemquerer MP]] | ||
| + | [[Category: Moraes CM]] | ||
| + | [[Category: Pilo-Veloso D]] | ||
| + | [[Category: Resende JM]] | ||
| + | [[Category: Valente A]] | ||
| + | [[Category: Verly RM]] | ||
Current revision
Structure and membrane interactions of the antibiotic peptide dermadistinctin K by multidimensional solution and oriented 15N and 31P solid-state NMR spectroscopy
| |||||||||||
