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| | ==THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB== | | ==THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB== |
| - | <StructureSection load='1cix' size='340' side='right' caption='[[1cix]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | + | <StructureSection load='1cix' size='340' side='right'caption='[[1cix]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1cix]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CIX FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cix]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tachypleus_tridentatus Tachypleus tridentatus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CIX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CIX 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=1cix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cix OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cix RCSB], [http://www.ebi.ac.uk/pdbsum/1cix PDBsum]</span></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 24 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=1cix FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cix OCA], [https://pdbe.org/1cix PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cix RCSB], [https://www.ebi.ac.uk/pdbsum/1cix PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cix ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/TACA2_TACTR TACA2_TACTR]] Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC(50) is 4.2 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.5 ug/ml)) than Gram-negative bacteria (E.coli (IC(50) is 25 ug/ml)). Binds to chitin (8.4 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. | + | [https://www.uniprot.org/uniprot/TACA2_TACTR TACA2_TACTR] Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC(50) is 4.2 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.5 ug/ml)) than Gram-negative bacteria (E.coli (IC(50) is 25 ug/ml)). Binds to chitin (8.4 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> |
| | </div> | | </div> |
| | + | <div class="pdbe-citations 1cix" style="background-color:#fffaf0;"></div> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Large Structures]] |
| | [[Category: Tachypleus tridentatus]] | | [[Category: Tachypleus tridentatus]] |
| - | [[Category: Demura, M]] | + | [[Category: Demura M]] |
| - | [[Category: Fujitani, N]] | + | [[Category: Fujitani N]] |
| - | [[Category: Kawabata, S]] | + | [[Category: Kawabata S]] |
| - | [[Category: Kawano, K]] | + | [[Category: Kawano K]] |
| - | [[Category: Kumaki, Y]] | + | [[Category: Kumaki Y]] |
| - | [[Category: Nitta, K]] | + | [[Category: Nitta K]] |
| - | [[Category: Osaki, T]] | + | [[Category: Osaki T]] |
| - | [[Category: Antimicrobial peptide]]
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| - | [[Category: Chitin-binding peptide]]
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| Structural highlights
Function
TACA2_TACTR Exhibits stronger antimicrobial activity against the Gram-positive bacteria (S.aureus (IC(50) is 4.2 ug/ml)) and fungi (C.albicans (IC(50) is 3.0 ug/ml) and P.pastoris (IC(50) is 0.5 ug/ml)) than Gram-negative bacteria (E.coli (IC(50) is 25 ug/ml)). Binds to chitin (8.4 uM are required to obtain 50% of binding). Does not cause hemolysis on sheep erythrocytes. Has no blocking activity on the P-type calcium channel.
Publication Abstract from PubMed
The solution structure of antimicrobial peptide tachystatin A from the Japanese horseshoe crab (Tachypleus tridentatus) was determined by two-dimensional nuclear magnetic resonance measurements and distance-restrained simulated annealing calculations. The correct pairs of disulfide bonds were also confirmed in this study. The obtained structure has a cysteine-stabilized triple-stranded beta-sheet as a dominant secondary structure and shows an amphiphilic folding observed in many membrane-interactive peptides. Interestingly, tachystatin A shares structural similarities with the calcium channel antagonist omega-agatoxin IVA isolated from spider toxin and mammalian defensins, and we predicted that omega-agatoxin IVA also have the antifungal activity. These structural comparisons and functional correspondences suggest that tachystatin A and omega-agatoxin IVA may exert the antimicrobial activity in a manner similar to defensins, and we have confirmed such activity using fungal culture assays. Furthermore, tachystatin A is a chitin-binding peptide, and omega-agatoxin IVA also showed chitin-binding activities in this study. Tachystatin A and omega-agatoxin IVA showed no structural homology with well known chitin-binding motifs, suggesting that their structures belong to a novel family of chitin-binding peptides. Comparison of their structures with those of cellulose-binding proteins indicated that Phe(9) of tachystatin A might be an essential residue for binding to chitin.
Structure of the antimicrobial peptide tachystatin A.,Fujitani N, Kawabata S, Osaki T, Kumaki Y, Demura M, Nitta K, Kawano K J Biol Chem. 2002 Jun 28;277(26):23651-7. Epub 2002 Apr 16. PMID:11959852[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Fujitani N, Kawabata S, Osaki T, Kumaki Y, Demura M, Nitta K, Kawano K. Structure of the antimicrobial peptide tachystatin A. J Biol Chem. 2002 Jun 28;277(26):23651-7. Epub 2002 Apr 16. PMID:11959852 doi:http://dx.doi.org/10.1074/jbc.M111120200
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