2b68

From Proteopedia

(Difference between revisions)

Current revision

Solution structure of the recombinant Crassostrea gigas defensin

Structural highlights

2b68 is a 1 chain structure with sequence from Crassostrea gigas. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR, 10 models
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

DEFCG_MAGGI Antibacterial peptide mostly active against Gram-positive bacteria (M.lysodeikticus, S.aureus, and the marine bacteria, B.stationis, and M.maritypicum) (PubMed:16246846). It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt cell membranes (PubMed:20605792). Is noticeably more potent than Cg-Defh1 (PubMed:20605792). It shows no or limited activities against Gram-negative bacteria and filamentous fungi (PubMed:16246846).^[1] ^[2]

Publication Abstract from PubMed

In invertebrates, defensins were found in arthropods and in the mussels. Here, we report for the first time the identification and characterization of a defensin (Cg-Def) from an oyster. Cg-def mRNA was isolated from Crassostrea gigas mantle using an expressed sequence tag approach. To gain insight into potential roles of Cg-Def in oyster immunity, we produced the recombinant peptide in Escherichia coli, characterized its antimicrobial activities, determined its solution structure by NMR spectroscopy, and quantified its gene expression in vivo following bacterial challenge of oysters. Recombinant Cg-Def was active in vitro against Gram-positive bacteria but showed no or limited activities against Gram-negative bacteria and fungi. The activity of Cg-Def was retained in vitro at a salt concentration similar to that of seawater. The Cg-Def structure shares the so-called cystine-stabilized alpha-beta motif (CS-alphabeta) with arthropod defensins but is characterized by the presence of an additional disulfide bond, as previously observed in the mussel defensin (MGD-1). Nevertheless, despite a similar global fold, the Cg-Def and MGD-1 structures mainly differ by the size of their loops and by the presence of two aspartic residues in Cg-Def. Distribution of Cg-def mRNA in various oyster tissues revealed that Cg-def is mainly expressed in mantle edge where it was detected by mass spectrometry analyses. Furthermore, we observed that the Cg-def messenger concentration was unchanged after bacterial challenge. Our results suggest that Cg-def gene is continuously expressed in the mantle and would play a key role in oyster by providing a first line of defense against pathogen colonization.

Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression.,Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, Escoubas JM, Bulet P, Gonzalez M, Lelong C, Favrel P, Bachere E J Biol Chem. 2006 Jan 6;281(1):313-23. Epub 2005 Oct 24. PMID:16246846^[3]

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

References

↑ Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, Escoubas JM, Bulet P, Gonzalez M, Lelong C, Favrel P, Bachere E. Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression. J Biol Chem. 2006 Jan 6;281(1):313-23. Epub 2005 Oct 24. PMID:16246846 doi:http://dx.doi.org/M510850200
↑ Schmitt P, Wilmes M, Pugnière M, Aumelas A, Bachère E, Sahl HG, Schneider T, Destoumieux-Garzón D. Insight into invertebrate defensin mechanism of action: oyster defensins inhibit peptidoglycan biosynthesis by binding to lipid II. J Biol Chem. 2010 Sep 17;285(38):29208-16. PMID:20605792 doi:10.1074/jbc.M110.143388
↑ Gueguen Y, Herpin A, Aumelas A, Garnier J, Fievet J, Escoubas JM, Bulet P, Gonzalez M, Lelong C, Favrel P, Bachere E. Characterization of a defensin from the oyster Crassostrea gigas. Recombinant production, folding, solution structure, antimicrobial activities, and gene expression. J Biol Chem. 2006 Jan 6;281(1):313-23. Epub 2005 Oct 24. PMID:16246846 doi:http://dx.doi.org/M510850200

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2b68"

@@ Line 4: / Line 4: @@
 == Structural highlights ==
 <table><tr><td colspan='2'>[[2b68]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Crassostrea_gigas Crassostrea gigas]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B68 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B68 FirstGlance]. <br>
-</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 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=2b68 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b68 OCA], [https://pdbe.org/2b68 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b68 RCSB], [https://www.ebi.ac.uk/pdbsum/2b68 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b68 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[https://www.uniprot.org/uniprot/DEFCG_CRAGI DEFCG_CRAGI] Antibacterial peptide mostly active against Gram-positive bacteria (M.lysodeikticus, S.aureus, and the marine bacteria, B.stationis, and M.maritypicum) (PubMed:16246846). It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt cell membranes (PubMed:20605792). Is noticeably more potent than Cg-Defh1 (PubMed:20605792). It shows no or limited activities against Gram-negative bacteria and filamentous fungi (PubMed:16246846).<ref>PMID:16246846</ref> <ref>PMID:20605792</ref>
+[https://www.uniprot.org/uniprot/DEFCG_MAGGI DEFCG_MAGGI] Antibacterial peptide mostly active against Gram-positive bacteria (M.lysodeikticus, S.aureus, and the marine bacteria, B.stationis, and M.maritypicum) (PubMed:16246846). It acts by selectively inhibiting peptidoglycan biosynthesis through complex formation with the cell wall precursor lipid II (1:1 molar ratio) thus inhibiting cell wall synthesis (PubMed:20605792). It does not disrupt cell membranes (PubMed:20605792). Is noticeably more potent than Cg-Defh1 (PubMed:20605792). It shows no or limited activities against Gram-negative bacteria and filamentous fungi (PubMed:16246846).<ref>PMID:16246846</ref> <ref>PMID:20605792</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==

2b68

From Proteopedia

Current revision

Solution structure of the recombinant Crassostrea gigas defensin

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

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