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PDBsum entry 1i2u
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Antifungal protein PDB id
1i2u

 

 

 

 

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Contents
Protein chain
44 a.a.
PDB id:
1i2u
Name: Antifungal protein
Title: Nmr solution structures of antifungal heliomicin
Structure: Defensin heliomicin. Chain: a. Engineered: yes
Source: Heliothis virescens. Tobacco budworm. Organism_taxid: 7102. Expressed in: saccharomyces cerevisiae. Expression_system_taxid: 4932.
NMR struc: 18 models
Authors: M.Lamberty,A.Caille,C.Landon,S.Tassin-Moindrot,C.Hetru,P.Bulet, F.Vovelle
Key ref:
M.Lamberty et al. (2001). Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities. Biochemistry, 40, 11995-12003. PubMed id: 11580275 DOI: 10.1021/bi0103563
Date:
12-Feb-01     Release date:   12-Feb-02    
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
P81544  (DEFN_HELVI) -  Defensin heliomicin from Heliothis virescens
Seq:
Struc: 		44 a.a.
44 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi0103563 Biochemistry 40:11995-12003 (2001)
PubMed id: 11580275  
 
 
Solution structures of the antifungal heliomicin and a selected variant with both antibacterial and antifungal activities.
M.Lamberty, A.Caille, C.Landon, S.Tassin-Moindrot, C.Hetru, P.Bulet, F.Vovelle.
 
  ABSTRACT  
 
In response to an experimental infection, the lepidopteran Heliothis virescens produces an antifungal protein named heliomicin. Heliomicin displays sequence similarities with antifungal plant defensins and antibacterial or antifungal insect defensins. To gain information about the structural elements required for either antifungal or antibacterial activity, heliomicin and selected point-mutated variants were expressed in yeast as fusion proteins. The effects of mutations, defined by comparing the primary structure of heliomicin with the sequences of members of the insect defensin family, were analyzed using antibacterial and antifungal assays. One of the variants shows significant activity against Gram-positive bacteria while remaining efficient against fungi. The three-dimensional structures of this variant and of the wild-type protein were determined by two-dimensional (1)H NMR to establish a correlation between structure and antibacterial or antifungal activity. Wild-type and mutated heliomicins adopt a similar scaffold, including the so-called cysteine-stabilized alphabeta motif. A comparison of their structures with other defensin-type molecules indicates that common hydrophobic characteristics can be assigned to all the antifungal proteins. A comparative analysis of various structural features of heliomicin mutant and of antibacterial defensins enables common properties to be assessed, which will help to design new mutants with increased antibacterial activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
17716729 B.J.Cuthbertson, L.J.Deterding, J.G.Williams, K.B.Tomer, K.Etienne, P.J.Blackshear, E.E.Büllesbach, and P.S.Gross (2008).
Diversity in penaeidin antimicrobial peptide form and function.
  Dev Comp Immunol, 32, 167-181.  
17340092 A.M.Aerts, K.Thevissen, S.M.Bresseleers, J.Sels, P.Wouters, B.P.Cammue, and I.E.François (2007).
Arabidopsis thaliana plants expressing human beta-defensin-2 are more resistant to fungal attack: functional homology between plant and human defensins.
  Plant Cell Rep, 26, 1391-1398.  
14978308 C.Landon, F.Barbault, M.Legrain, L.Menin, M.Guenneugues, V.Schott, F.Vovelle, and J.L.Dimarcq (2004).
Lead optimization of antifungal peptides with 3D NMR structures analysis.
  Protein Sci, 13, 703-713.
PDB codes: 1ozz 1p00 1p0a
14604982 K.Thevissen, D.C.Warnecke, I.E.François, M.Leipelt, E.Heinz, C.Ott, U.Zähringer, B.P.Thomma, K.K.Ferket, and B.P.Cammue (2004).
Defensins from insects and plants interact with fungal glucosylceramides.
  J Biol Chem, 279, 3900-3905.  
14996645 L.Zhang, and T.J.Falla (2004).
Cationic antimicrobial peptides - an update.
  Expert Opin Investig Drugs, 13, 97.  
15199962 P.Bulet, R.Stöcklin, and L.Menin (2004).
Anti-microbial peptides: from invertebrates to vertebrates.
  Immunol Rev, 198, 169-184.  
14661954 F.Barbault, C.Landon, M.Guenneugues, J.P.Meyer, V.Schott, J.L.Dimarcq, and F.Vovelle (2003).
Solution structure of Alo-3: a new knottin-type antifungal peptide from the insect Acrocinus longimanus.
  Biochemistry, 42, 14434-14442.
PDB code: 1q3j
12676931 H.Hemmi, J.Ishibashi, T.Tomie, and M.Yamakawa (2003).
Structural basis for new pattern of conserved amino acid residues related to chitin-binding in the antifungal peptide from the coconut rhinoceros beetle Oryctes rhinoceros.
  J Biol Chem, 278, 22820-22827.
PDB code: 1iyc
14556622 L.Jouvensal, L.Quillien, E.Ferrasson, Y.Rahbé, J.Guéguen, and F.Vovelle (2003).
PA1b, an insecticidal protein extracted from pea seeds (Pisum sativum): 1H-2-D NMR study and molecular modeling.
  Biochemistry, 42, 11915-11923.
PDB code: 1p8b
12592014 P.Da Silva, L.Jouvensal, M.Lamberty, P.Bulet, A.Caille, and F.Vovelle (2003).
Solution structure of termicin, an antimicrobial peptide from the termite Pseudacanthotermes spiniger.
  Protein Sci, 12, 438-446.
PDB code: 1mm0
12413797 J.Vizioli, and M.Salzet (2002).
Antimicrobial peptides from animals: focus on invertebrates.
  Trends Pharmacol Sci, 23, 494-496.  
11856345 N.Mandard, P.Bulet, A.Caille, S.Daffre, and F.Vovelle (2002).
The solution structure of gomesin, an antimicrobial cysteine-rich peptide from the spider.
  Eur J Biochem, 269, 1190-1198.
PDB code: 1kfp
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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