1kfp

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the antimicrobial 18-residue gomesin

Structural highlights

1kfp is a 1 chain structure with sequence from Acanthoscurria gomesiana. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 20 models
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

GOME_ACAGO Active against several Gram-positive bacteria such as Bacillus spp, Staphylococcus spp and E.faecalis, several Gram-negative bacteria such as E.coli, K.pneumoniae, P.aeruginosa and Salmonella spp, filamentous fungi such as N.crassa, T.viridae and yeasts such as C.albicans. It is active against the parasite L.amazonensis as well. It shows hemolytic activity.^[1]

Publication Abstract from PubMed

Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has been determined using proton two-dimensional NMR (2D-NMR) and restrained molecular dynamics calculations. The global fold of gomesin consists in a well-resolved two-stranded antiparallel betasheet connected by a noncanonical betaturn. A comparison between the structures of gomesin and protegrin-1 from porcine and androctonin from scorpion outlines several common features in the distribution of hydrophobic and hydrophilic residues. The N- and C-termini, the betaturn and one face of the betasheet are hydrophilic, but the hydrophobicity of the other face depends on the peptide. The similarities suggest that the molecules interact with membranes in an analogous manner. The importance of the intramolecular disulfide bridges in the biological activity of gomesin is being investigated.

The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.,Mandard N, Bulet P, Caille A, Daffre S, Vovelle F Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345^[2]

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

References

↑ Silva PI Jr, Daffre S, Bulet P. Isolation and characterization of gomesin, an 18-residue cysteine-rich defense peptide from the spider Acanthoscurria gomesiana hemocytes with sequence similarities to horseshoe crab antimicrobial peptides of the tachyplesin family. J Biol Chem. 2000 Oct 27;275(43):33464-70. PMID:10942757 doi:http://dx.doi.org/10.1074/jbc.M001491200
↑ Mandard N, Bulet P, Caille A, Daffre S, Vovelle F. The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider. Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345

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/1kfp"

@@ Line 1: / Line 1: @@
-[[Image:1kfp.gif|left|200px]]<br /><applet load="1kfp" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1kfp" />
-'''Solution structure of the antimicrobial 18-residue gomesin'''<br />
-==Overview==
+==Solution structure of the antimicrobial 18-residue gomesin==
-Gomesin is the first peptide isolated from spider exhibiting antimicrobial, activities. This highly cationic peptide is composed of 18 amino-acid, residues including four cysteines forming two disulfide linkages. The, solution structure of gomesin has been determined using proton, two-dimensional NMR (2D-NMR) and restrained molecular dynamics, calculations. The global fold of gomesin consists in a well-resolved, two-stranded antiparallel betasheet connected by a noncanonical betaturn., A comparison between the structures of gomesin and protegrin-1 from, porcine and androctonin from scorpion outlines several common features in, the distribution of hydrophobic and hydrophilic residues. The N- and, C-termini, the betaturn and one face of the betasheet are hydrophilic, but, the hydrophobicity of the other face depends on the peptide. The, similarities suggest that the molecules interact with membranes in an, analogous manner. The importance of the intramolecular disulfide bridges, in the biological activity of gomesin is being investigated.
+<StructureSection load='1kfp' size='340' side='right'caption='[[1kfp]]' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1kfp]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Acanthoscurria_gomesiana Acanthoscurria gomesiana]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KFP 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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</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=1kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kfp OCA], [https://pdbe.org/1kfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kfp RCSB], [https://www.ebi.ac.uk/pdbsum/1kfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kfp ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/GOME_ACAGO GOME_ACAGO] Active against several Gram-positive bacteria such as Bacillus spp, Staphylococcus spp and E.faecalis, several Gram-negative bacteria such as E.coli, K.pneumoniae, P.aeruginosa and Salmonella spp, filamentous fungi such as N.crassa, T.viridae and yeasts such as C.albicans. It is active against the parasite L.amazonensis as well. It shows hemolytic activity.<ref>PMID:10942757</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Gomesin is the first peptide isolated from spider exhibiting antimicrobial activities. This highly cationic peptide is composed of 18 amino-acid residues including four cysteines forming two disulfide linkages. The solution structure of gomesin has been determined using proton two-dimensional NMR (2D-NMR) and restrained molecular dynamics calculations. The global fold of gomesin consists in a well-resolved two-stranded antiparallel betasheet connected by a noncanonical betaturn. A comparison between the structures of gomesin and protegrin-1 from porcine and androctonin from scorpion outlines several common features in the distribution of hydrophobic and hydrophilic residues. The N- and C-termini, the betaturn and one face of the betasheet are hydrophilic, but the hydrophobicity of the other face depends on the peptide. The similarities suggest that the molecules interact with membranes in an analogous manner. The importance of the intramolecular disulfide bridges in the biological activity of gomesin is being investigated.
-==About this Structure==
+The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.,Mandard N, Bulet P, Caille A, Daffre S, Vovelle F Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:11856345<ref>PMID:11856345</ref>
-KFP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1KFP OCA].
-==Reference==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider., Mandard N, Bulet P, Caille A, Daffre S, Vovelle F, Eur J Biochem. 2002 Feb;269(4):1190-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11856345 11856345]
+</div>
-[[Category: Single protein]]
+<div class="pdbe-citations 1kfp" style="background-color:#fffaf0;"></div>
-[[Category: Bulet, P.]]
+== References ==
-[[Category: Caille, A.]]
+<references/>
-[[Category: Daffre, S.]]
+__TOC__
-[[Category: Mandard, N.]]
+</StructureSection>
-[[Category: Vovelle, F.]]
+[[Category: Acanthoscurria gomesiana]]
-[[Category: NH2]]
+[[Category: Large Structures]]
-[[Category: beta-sheet]]
+[[Category: Bulet P]]
-[[Category: disulfide bridges]]
+[[Category: Caille A]]
-[[Category: hairpin-like]]
+[[Category: Daffre S]]
+[[Category: Mandard N]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 19:10:23 2007''
+[[Category: Vovelle F]]

1kfp

From Proteopedia

Current revision

Solution structure of the antimicrobial 18-residue gomesin

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

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