This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.

1ueo

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Revision as of 04:09, 11 September 2015

Solution structure of the [T8A]-Penaeidin-3

Structural highlights

1ueo is a 1 chain structure with sequence from Litva. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[PEN3A_LITVA] Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin-binding activity.^[1] ^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Penaeidins are a family of antimicrobial peptides of 47-63 residues isolated from several species of shrimp. These peptides display a proline-rich domain (N-terminal part) and a cysteine-rich domain (C-terminal part) stabilized by three conserved disulfide bonds whose arrangement has not yet been characterized. The recombinant penaeidin-3a of Litopenaeus vannamei (63 residues) and its [T8A]-Pen-3a analogue were produced in Saccharomyces cerevisiae and showed similar antimicrobial activity. The solution structure of the [T8A]-Pen-3a analogue was determined by using two-dimensional 1H NMR and simulated annealing calculations. The proline-rich domain, spanning residues 1-28 was found to be unconstrained. In contrast, the cysteine-rich domain, spanning residues 29-58, displays a well defined structure, which consists of an amphipathic helix (41-50) linked to the upstream and the downstream coils by two disulfide bonds (Cys32-Cys47 and Cys48-Cys55). These two coils are in turn linked together by the third disulfide bond (Cys36-Cys54). Such a disulfide bond packing, which is in agreement with the analysis of trypsin digests by ESI-MS, contributes to the highly hydrophobic core. Side chains of Arg45 and Arg50, which belong to the helix, and side chains of Arg37 and Arg53, which belong to the upstream and the downstream coils, are located in two opposite parts of this globular and compact structure. The environment of these positively charged residues, either by hydrophobic clusters at the surface of the cysteine-rich domain or by sequential hydrophobic residues in the unconstrained proline-rich domain, gives rise to the amphipathic character required for antimicrobial peptides. We hypothesize that the antimicrobial activity of penaeidins can be explained by a cooperative effect between the proline-rich and cysteine-rich features simultaneously present in their sequences.

Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide.,Yang Y, Poncet J, Garnier J, Zatylny C, Bachere E, Aumelas A J Biol Chem. 2003 Sep 19;278(38):36859-67. Epub 2003 Jul 3. PMID:12842879^[3]

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

References

↑ Destoumieux D, Bulet P, Strub JM, Van Dorsselaer A, Bachere E. Recombinant expression and range of activity of penaeidins, antimicrobial peptides from penaeid shrimp. Eur J Biochem. 1999 Dec;266(2):335-46. PMID:10561573
↑ Destoumieux D, Bulet P, Loew D, Van Dorsselaer A, Rodriguez J, Bachere E. Penaeidins, a new family of antimicrobial peptides isolated from the shrimp Penaeus vannamei (Decapoda). J Biol Chem. 1997 Nov 7;272(45):28398-406. PMID:9353298
↑ Yang Y, Poncet J, Garnier J, Zatylny C, Bachere E, Aumelas A. Solution structure of the recombinant penaeidin-3, a shrimp antimicrobial peptide. J Biol Chem. 2003 Sep 19;278(38):36859-67. Epub 2003 Jul 3. PMID:12842879 doi:10.1074/jbc.M305450200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ueo"

@@ Line 2: / Line 2: @@
 <StructureSection load='1ueo' size='340' side='right' caption='[[1ueo]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ueo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Litopenaeus_vannamei Litopenaeus vannamei]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UEO FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1ueo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Litva Litva]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UEO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1UEO 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=1ueo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1ueo RCSB], [http://www.ebi.ac.uk/pdbsum/1ueo PDBsum]</span></td></tr>
+</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=1ueo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ueo OCA], [http://pdbe.org/1ueo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ueo RCSB], [http://www.ebi.ac.uk/pdbsum/1ueo PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/PEN3A_PENVA PEN3A_PENVA]] Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin-binding activity.<ref>PMID:9353298</ref> <ref>PMID:10561573</ref>
+[[http://www.uniprot.org/uniprot/PEN3A_LITVA PEN3A_LITVA]] Antibacterial activity against M.luteus and E.coli bacteria. Antifungal activity against N.crassa and F.oxysporum. Presents chitin-binding activity.<ref>PMID:10561573</ref> <ref>PMID:9353298</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 25: / Line 25: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1ueo" style="background-color:#fffaf0;"></div>
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Litopenaeus vannamei]]
+[[Category: Litva]]
 [[Category: Aumelas, A]]
 [[Category: Bachere, E]]

1ueo

From Proteopedia

Revision as of 04:09, 11 September 2015

Solution structure of the [T8A]-Penaeidin-3

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox