1cix

From Proteopedia

(Difference between revisions)

Current revision

THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB

Structural highlights

1cix is a 1 chain structure with sequence from Tachypleus tridentatus. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 24 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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

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/1cix"

@@ Line 1: / Line 1: @@
-{{Seed}}
-[[Image:1cix.png|left|200px]]
-<!--
+==THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB==
-The line below this paragraph, containing "STRUCTURE_1cix", creates the "Structure Box" on the page.
+<StructureSection load='1cix' size='340' side='right'caption='[[1cix]]' scene=''>
-You may change the PDB parameter (which sets the PDB file loaded into the applet)
+== Structural highlights ==
-or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+<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>
-or leave the SCENE parameter empty for the default display.
+</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>
-{{STRUCTURE_1cix|  PDB=1cix  |  SCENE=  }}
+</table>
+== Function ==
+[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;">
+== 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.
-===THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB===
+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<ref>PMID:11959852</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-<!--
+</div>
-The line below this paragraph, {{ABSTRACT_PUBMED_11959852}}, adds the Publication Abstract to the page
+<div class="pdbe-citations 1cix" style="background-color:#fffaf0;"></div>
-(as it appears on PubMed at http://www.pubmed.gov), where 11959852 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_11959852}}
+__TOC__
+</StructureSection>
-==About this Structure==
+[[Category: Large Structures]]
-CIX is a [[Single protein]] structure of 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].
-==Reference==
-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:[http://www.ncbi.nlm.nih.gov/pubmed/11959852 11959852]
-[[Category: Single protein]]
 [[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]]
-[[Category: Chitin-binding peptide]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 20:48:33 2008''

1cix

From Proteopedia

Current revision

THREE-DIMENSIONAL STRUCTURE OF ANTIMICROBIAL PEPTIDE TACHYSTATIN A ISOLATED FROM HORSESHOE CRAB

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox