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1fjn

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Revision as of 10:47, 13 September 2017

SOLUTION STRUCTURE AND ACTIVITY OF THE FOUR DISULFIDE BOND MEDITERRANEAN MUSSEL DEFENSIN MGD-1

Structural highlights

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

Function

[DEFI_MYTGA] Active against both Gram-positive and Gram-negative bacteria but is not cytotoxic towards human erythrocytes or protozoa.^[1]

Publication Abstract from PubMed

MGD-1 is a 39-residue defensin-like peptide isolated from the edible Mediterranean mussel, Mytilus galloprovincialis. This peptide is characterized by the presence of four disulfide bonds. We report here its solid-phase synthesis and an easy way to improve the yield of the four native disulfide bonds. Synthetic and native MGD-1 display similar antibacterial activity, suggesting that the hydroxylation of Trp28 observed in native MGD-1 is not involved in the antimicrobial effect. The three-dimensional solution structure of MGD-1 has been established using (1)H NMR and mainly consists of a helical part (Asn7-Ser16) and two antiparallel beta-strands (Arg20-Cys25 and Cys33-Arg37), together giving rise to the common cystine-stabilized alpha-beta motif frequently observed in scorpion toxins. In MGD-1, the cystine-stabilized alpha-beta motif is stabilized by four disulfide bonds (Cys4-Cys25, Cys10-Cys33, Cys14-Cys35, and Cys21-Cys38), instead of by the three disulfide bonds commonly found in arthropod defensins. Except for the Cys21-Cys38 disulfide bond which is solvent-exposed, the three others belong to the particularly hydrophobic core of the highly constrained structure. Moreover, the C4-P5 amide bond in the cis conformation characterizes the MGD-1 structure. MGD-1 and insect defensin A possess similar bactericidal anti-Gram-positive activity, suggesting that the fourth disulfide bond of MGD-1 is not essential for the biological activity. In agreement with the general features of antibacterial peptides, the MGD-1 and defensin A structures display a typical distribution of positively charged and hydrophobic side chains. The positively charged residues of MGD-1 are located in three clusters. For these two defensin peptides isolated from insects and mollusks, it appears that the rather well conserved location of certain positively charged residues and of the large hydrophobic cluster are enough to generate the bactericidal potency and the Gram-positive specificity.

Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1).,Yang YS, Mitta G, Chavanieu A, Calas B, Sanchez JF, Roch P, Aumelas A Biochemistry. 2000 Nov 28;39(47):14436-47. PMID:11087396^[2]

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

References

↑ Hubert F, Noel T, Roch P. A member of the arthropod defensin family from edible Mediterranean mussels (Mytilus galloprovincialis) Eur J Biochem. 1996 Aug 15;240(1):302-6. PMID:8925841
↑ Yang YS, Mitta G, Chavanieu A, Calas B, Sanchez JF, Roch P, Aumelas A. Solution structure and activity of the synthetic four-disulfide bond Mediterranean mussel defensin (MGD-1). Biochemistry. 2000 Nov 28;39(47):14436-47. PMID:11087396

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/1fjn"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE AND ACTIVITY OF THE FOUR DISULFIDE BOND MEDITERRANEAN MUSSEL DEFENSIN MGD-1==
 <StructureSection load='1fjn' size='340' side='right' caption='[[1fjn]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
 == Structural highlights ==
 <table><tr><td colspan='2'>[[1fjn]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FJN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FJN 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=1fjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjn OCA], [http://pdbe.org/1fjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fjn RCSB], [http://www.ebi.ac.uk/pdbsum/1fjn 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=1fjn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fjn OCA], [http://pdbe.org/1fjn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fjn RCSB], [http://www.ebi.ac.uk/pdbsum/1fjn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fjn ProSAT]</span></td></tr>
 </table>
 == Function ==

1fjn

From Proteopedia

Revision as of 10:47, 13 September 2017

SOLUTION STRUCTURE AND ACTIVITY OF THE FOUR DISULFIDE BOND MEDITERRANEAN MUSSEL DEFENSIN MGD-1

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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