1cz6
From Proteopedia
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| - | [[Image:1cz6.jpg|left|200px]]<br /><applet load="1cz6" size="350" color="white" frame="true" align="right" spinBox="true" | ||
| - | caption="1cz6" /> | ||
| - | '''SOLUTION STRUCTURE OF ANDROCTONIN'''<br /> | ||
| - | == | + | ==SOLUTION STRUCTURE OF ANDROCTONIN== |
| + | <StructureSection load='1cz6' size='340' side='right'caption='[[1cz6]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[1cz6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Androctonus_australis Androctonus australis]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CZ6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CZ6 FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 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=1cz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cz6 OCA], [https://pdbe.org/1cz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cz6 RCSB], [https://www.ebi.ac.uk/pdbsum/1cz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cz6 ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ANDT_ANDAU ANDT_ANDAU] Active against both bacteria (Gram-positive and Gram-negative) and filamentous fungi. Acts on the membrane of the bacterial cells. It destabilize a membrane by modifying its properties. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria and fungi. It contains 25 amino acids including four cysteine residues forming two disulfide bridges. We report here on the determination of its solution structure by conventional two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling using distance geometry and molecular dynamics methods. The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn. A comparison with the structure of tachyplesin I (horseshoe crab) reveals that the amphiphilic character of the protein surface of this homologous peptide is not observed in androctonin. We have undertaken a 200-ps molecular dynamics simulation study on a system including one androctonin molecule and a monolayer of DMPG (1,2-dimyristoylphosphatidylglycerol) lipids. On the basis of this simulation, the first steps of the membrane permeabilization process are discussed. | Androctonin is a highly cationic antimicrobial peptide from scorpion exhibiting a broad spectrum of activities against bacteria and fungi. It contains 25 amino acids including four cysteine residues forming two disulfide bridges. We report here on the determination of its solution structure by conventional two-dimensional (2D) 1H-NMR spectroscopy and molecular modelling using distance geometry and molecular dynamics methods. The structure of androctonin involves a well-defined highly twisted anti-parallel beta-sheet with strands connected by a more variable positively charged turn. A comparison with the structure of tachyplesin I (horseshoe crab) reveals that the amphiphilic character of the protein surface of this homologous peptide is not observed in androctonin. We have undertaken a 200-ps molecular dynamics simulation study on a system including one androctonin molecule and a monolayer of DMPG (1,2-dimyristoylphosphatidylglycerol) lipids. On the basis of this simulation, the first steps of the membrane permeabilization process are discussed. | ||
| - | + | Androctonin, a novel antimicrobial peptide from scorpion Androctonus australis: solution structure and molecular dynamics simulations in the presence of a lipid monolayer.,Mandard N, Sy D, Maufrais C, Bonmatin JM, Bulet P, Hetru C, Vovelle F J Biomol Struct Dyn. 1999 Oct;17(2):367-80. PMID:10563585<ref>PMID:10563585</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| + | <div class="pdbe-citations 1cz6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
[[Category: Androctonus australis]] | [[Category: Androctonus australis]] | ||
| - | [[Category: | + | [[Category: Large Structures]] |
| - | [[Category: Mandard | + | [[Category: Mandard N]] |
| - | [[Category: Vovelle | + | [[Category: Vovelle F]] |
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Current revision
SOLUTION STRUCTURE OF ANDROCTONIN
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