2l5r

From Proteopedia

(Difference between revisions)

Revision as of 12:11, 15 November 2023

Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C

Structural highlights

2l5r is a 1 chain structure with sequence from Alytes obstetricans. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ATI1C_ALYOB Antibacterial peptide with amphipathic alpha-helical structure that shows selective growth-inhibitory activity against Gram-negative bacteria but low hemolytic activity against human erythrocytes (LC(50)=145-220 uM) (PubMed:19463738, PubMed:21565166). It is moderately active against the Gram-negative bacteria E.coli (MIC=25 uM), K.pneumoniae (MIC=50 uM), P.aeruginosa (MIC=25 uM), A.baumannii (MIC=6 uM), and is weaky active against the Gram-positive S.aureus (MIC=100-250 uM) (PubMed:19463738, PubMed:21565166).^[1] ^[2]

Publication Abstract from PubMed

Alyteserin-1c (GLKEIFKAGLGSLVKGIAAHVAS.NH(2)), first isolated from skin secretions of the midwife toad Alytes obstetricans, shows selective growth-inhibitory activity against Gram-negative bacteria. The structures of alyteserin-1c and its more potent and less haemolytic analogue [E4K]alyteserin-1c were investigated in various solution and membrane mimicking environments by proton NMR spectroscopy and molecular modelling. In aqueous solution, the peptide displays a lack of secondary structure but, in a 2,2,2-trifluoroethanol (TFE-d(3))-H(2)O solvent mixture, the structure is characterised by an extended alpha helix between residues Leu(2) and Val(21). Solution structural studies in the membrane mimicking environments, sodium dodecyl sulphate (SDS), dodecylphosphocholine (DPC), and 1,2-dihexanoyl-sn-glycero-3-phosphatidylcholine (DHPC) micelles, indicate that these peptides display an alpha helical structure between residues Lys(3) and Val(21). Positional studies of the peptides in SDS, DPC and DHPC media show that the N-terminal and central residues lie inside the micelle while C-terminal residues beyond Ala(19) do not interact with the micelles.

Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c.,Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM Biochim Biophys Acta. 2011 Aug;1808(8):1975-84. Epub 2011 Apr 30. PMID:21565166^[3]

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

References

↑ Conlon JM, Demandt A, Nielsen PF, Leprince J, Vaudry H, Woodhams DC. The alyteserins: two families of antimicrobial peptides from the skin secretions of the midwife toad Alytes obstetricans (Alytidae). Peptides. 2009 Jun;30(6):1069-73. PMID:19463738 doi:10.1016/j.peptides.2009.03.004
↑ Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM. Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c. Biochim Biophys Acta. 2011 Aug;1808(8):1975-84. Epub 2011 Apr 30. PMID:21565166 doi:10.1016/j.bbamem.2011.04.012
↑ Subasinghage AP, O'Flynn D, Conlon JM, Hewage CM. Conformational and membrane interaction studies of the antimicrobial peptide alyteserin-1c and its analogue [E4K]alyteserin-1c. Biochim Biophys Acta. 2011 Aug;1808(8):1975-84. Epub 2011 Apr 30. PMID:21565166 doi:10.1016/j.bbamem.2011.04.012

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/2l5r"

Categories: Alytes obstetricans | Large Structures | Conlon M | Hewage CM | Subasinghage AP

@@ Line 1: / Line 1: @@
 ==Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C==
-<StructureSection load='2l5r' size='340' side='right'caption='[[2l5r]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2l5r' size='340' side='right'caption='[[2l5r]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2l5r]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5R FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2l5r]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Alytes_obstetricans Alytes obstetricans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L5R OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L5R FirstGlance]. <br>
-</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=2l5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5r OCA], [https://pdbe.org/2l5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5r RCSB], [https://www.ebi.ac.uk/pdbsum/2l5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5r 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</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=2l5r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l5r OCA], [https://pdbe.org/2l5r PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l5r RCSB], [https://www.ebi.ac.uk/pdbsum/2l5r PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l5r ProSAT]</span></td></tr>
 </table>
+== Function ==
+[https://www.uniprot.org/uniprot/ATI1C_ALYOB ATI1C_ALYOB] Antibacterial peptide with amphipathic alpha-helical structure that shows selective growth-inhibitory activity against Gram-negative bacteria but low hemolytic activity against human erythrocytes (LC(50)=145-220 uM) (PubMed:19463738, PubMed:21565166). It is moderately active against the Gram-negative bacteria E.coli (MIC=25 uM), K.pneumoniae (MIC=50 uM), P.aeruginosa (MIC=25 uM), A.baumannii (MIC=6 uM), and is weaky active against the Gram-positive S.aureus (MIC=100-250 uM) (PubMed:19463738, PubMed:21565166).<ref>PMID:19463738</ref> <ref>PMID:21565166</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 22: @@
 __TOC__
 </StructureSection>
+[[Category: Alytes obstetricans]]
 [[Category: Large Structures]]
-[[Category: Conlon, M]]
+[[Category: Conlon M]]
-[[Category: Hewage, C M]]
+[[Category: Hewage CM]]
-[[Category: Subasinghage, A P]]
+[[Category: Subasinghage AP]]
-[[Category: Alpha helix]]
-[[Category: Antimicrobial protein]]

2l5r

From Proteopedia

Revision as of 12:11, 15 November 2023

Conformational and membrane interactins studies of antimicrobial peptide Alyteserin-1C

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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