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PDBsum entry 1gpt

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Plant toxin PDB id
1gpt

 

 

 

 

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Contents
Protein chain
47 a.a. *
* Residue conservation analysis
PDB id:
1gpt
Name: Plant toxin
Title: Solution structure of gamma 1-h and gamma 1-p thionins from barley and wheat endosperm determined by 1h-nmr: a structural motif common to toxic arthropod proteins
Structure: Gamma-1-h thionin. Chain: a. Engineered: yes
Source: Hordeum vulgare. Organism_taxid: 4513
NMR struc: 8 models
Authors: M.Bruix,M.A.Jimenez,J.Santoro,C.Gonzalez,F.J.Colilla,E.Mendez,M.Rico
Key ref:
M.Bruix et al. (1993). Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins. Biochemistry, 32, 715-724. PubMed id: 8380707 DOI: 10.1021/bi00053a041
Date:
29-Jul-92     Release date:   31-Oct-93    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P20230  (DEF1_HORVU) -  Defensin-like protein 1 from Hordeum vulgare
Seq:
Struc:
47 a.a.
47 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 

 
DOI no: 10.1021/bi00053a041 Biochemistry 32:715-724 (1993)
PubMed id: 8380707  
 
 
Solution structure of gamma 1-H and gamma 1-P thionins from barley and wheat endosperm determined by 1H-NMR: a structural motif common to toxic arthropod proteins.
M.Bruix, M.A.Jiménez, J.Santoro, C.González, F.J.Colilla, E.Méndez, M.Rico.
 
  ABSTRACT  
 
The complete assignment of the proton NMR spectra of the homologous gamma 1-hordothionin and gamma 1-purothionin (47 amino acids, 4 disulfide bridges) from barley and wheat, respectively, has been performed by two-dimensional sequence-specific methods. A total of 299 proton-proton distance constraints for gamma 1-H and 285 for gamma 1-P derived from NOESY spectra have been used to calculate the three-dimensional solution structures. Initial structures have been generated by distance geometry methods and further refined by dynamical simulated annealing calculations. Both proteins show identical secondary and tertiary structure with a well-defined triple-stranded antiparallel beta-sheet (residues 1-6, 31-34, and 39-47), an alpha-helix (residues 16-28), and the corresponding connecting loops. Three disulfide bridges are located in the hydrophobic core holding together the alpha-helix and the beta-sheet and forming a cysteine-stabilized alpha-helical (CSH) motif. Moreover, a clustering of positive charges is observed on the face of the beta-sheet opposite to the helix. The three-dimensional structures of the gamma-thionins differ remarkably from plant alpha- and beta-thionins and crambin. However, they show a higher structural analogy with scorpion toxins and insect defensins which also present the CSH motif.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
  20009545 H.U.Stotz, J.G.Thomson, and Y.Wang (2009).
Plant defensins: defense, development and application.
  Plant Signal Behav, 4, 1010-1012.  
18069950 N.Farrokhi, J.P.Whitelegge, and J.A.Brusslan (2008).
Plant peptides and peptidomics.
  Plant Biotechnol J, 6, 105-134.  
17211515 D.L.Laudencia-Chingcuanco, B.S.Stamova, F.M.You, G.R.Lazo, D.M.Beckles, and O.D.Anderson (2007).
Transcriptional profiling of wheat caryopsis development using cDNA microarrays.
  Plant Mol Biol, 63, 651-668.  
17444520 K.F.Lin, T.R.Lee, P.H.Tsai, M.P.Hsu, C.S.Chen, and P.C.Lyu (2007).
Structure-based protein engineering for alpha-amylase inhibitory activity of plant defensin.
  Proteins, 68, 530-540.
PDB code: 2gl1
16400645 M.E.Moghaddam, and H.Naderi-Manesh (2006).
Role of disulfide bonds in modulating internal motions of proteins to tune their function: molecular dynamics simulation of scorpion toxin Lqh III.
  Proteins, 63, 188-196.  
16736494 N.Y.Yount, A.S.Bayer, Y.Q.Xiong, and M.R.Yeaman (2006).
Advances in antimicrobial peptide immunobiology.
  Biopolymers, 84, 435-458.  
16544327 Y.J.Liu, C.S.Cheng, S.M.Lai, M.P.Hsu, C.S.Chen, and P.C.Lyu (2006).
Solution structure of the plant defensin VrD1 from mung bean and its possible role in insecticidal activity against bruchids.
  Proteins, 63, 777-786.
PDB code: 1ti5
16721719 Y.S.Shiau, S.B.Horng, C.S.Chen, P.T.Huang, C.Lin, Y.C.Hsueh, and K.L.Lou (2006).
Structural analysis of the unique insecticidal activity of novel mungbean defensin VrD1 reveals possibility of homoplasy evolution between plant defensins and scorpion neurotoxins.
  J Mol Recognit, 19, 441-450.  
15585533 E.Zhao, H.L.Liu, C.H.Tsai, H.K.Tsai, C.H.Chan, and C.Y.Kao (2005).
Cysteine separations profiles on protein sequences infer disulfide connectivity.
  Bioinformatics, 21, 1415-1420.  
16027978 M.Balandín, J.Royo, E.Gómez, L.M.Muniz, A.Molina, and G.Hueros (2005).
A protective role for the embryo surrounding region of the maize endosperm, as evidenced by the characterisation of ZmESR-6, a defensin gene specifically expressed in this region.
  Plant Mol Biol, 58, 269-282.  
16084753 P.B.Pelegrini, and O.L.Franco (2005).
Plant gamma-thionins: novel insights on the mechanism of action of a multi-functional class of defense proteins.
  Int J Biochem Cell Biol, 37, 2239-2253.  
12945044 C.C.Chuang, C.Y.Chen, J.M.Yang, P.C.Lyu, and J.K.Hwang (2003).
Relationship between protein structures and disulfide-bonding patterns.
  Proteins, 53, 1-5.  
12709056 G.Nicastro, L.Franzoni, C.de Chiara, A.C.Mancin, J.R.Giglio, and A.Spisni (2003).
Solution structure of crotamine, a Na+ channel affecting toxin from Crotalus durissus terrificus venom.
  Eur J Biochem, 270, 1969-1979.
PDB code: 1h5o
12835321 M.Mishima, S.Takayama, K.Sasaki, J.G.Jee, C.Kojima, A.Isogai, and M.Shirakawa (2003).
Structure of the male determinant factor for Brassica self-incompatibility.
  J Biol Chem, 278, 36389-36395.
PDB code: 1ugl
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
12112698 F.R.Melo, D.J.Rigden, O.L.Franco, L.V.Mello, M.B.Ary, M.F.Grossi de Sá, and C.Bloch (2002).
Inhibition of trypsin by cowpea thionin: characterization, molecular modeling, and docking.
  Proteins, 48, 311-319.  
12186551 H.Hemmi, T.Yoshida, T.Kumazaki, N.Nemoto, J.Hasegawa, F.Nishioka, Y.Kyogoku, H.Yokosawa, and Y.Kobayashi (2002).
Solution structure of ascidian trypsin inhibitor determined by nuclear magnetic resonance spectroscopy.
  Biochemistry, 41, 10657-10664.
PDB code: 1iw4
11952787 I.Huys, K.Dyason, E.Waelkens, F.Verdonck, J.van Zyl, J.du Plessis, G.J.Müller, J.van der Walt, E.Clynen, L.Schoofs, and J.Tytgat (2002).
Purification, characterization and biosynthesis of parabutoxin 3, a component of Parabuthus transvaalicus venom.
  Eur J Biochem, 269, 1854-1865.  
11856298 O.L.Franco, D.J.Rigden, F.R.Melo, and M.F.Grossi-De-Sá (2002).
Plant alpha-amylase inhibitors and their interaction with insect alpha-amylases.
  Eur J Biochem, 269, 397-412.  
12383115 Y.M.Sun, W.Liu, R.H.Zhu, C.Goudet, J.Tytgat, and D.C.Wang (2002).
Roles of disulfide bridges in scorpion toxin BmK M1 analyzed by mutagenesis.
  J Pept Res, 60, 247-256.  
11763131 L.Vila, V.Lacadena, P.Fontanet, A.Martinez del Pozo, and B.San Segundo (2001).
A protein from the mold Aspergillus giganteus is a potent inhibitor of fungal plant pathogens.
  Mol Plant Microbe Interact, 14, 1327-1331.  
11060677 A.J.De Lucca (2000).
Antifungal peptides: potential candidates for the treatment of fungal infections.
  Expert Opin Investig Drugs, 9, 273-299.  
11083062 C.Landon, A.Pajon, F.Vovelle, and P.Sodano (2000).
The active site of drosomycin, a small insect antifungal protein, delineated by comparison with the modeled structure of Rs-AFP2, a plant antifungal protein.
  J Pept Res, 56, 231-238.  
10103011 E.Kellenberger, G.Mer, C.Kellenberger, G.Marguerie, and J.F.Lefèvre (1999).
Solution structure of a conformationally constrained Arg-Gly-Asp-like motif inserted into the alpha/beta scaffold of leiurotoxin I.
  Eur J Biochem, 260, 810-817.  
10591099 F.Fant, W.F.Vranken, and F.A.Borremans (1999).
The three-dimensional solution structure of Aesculus hippocastanum antimicrobial protein 1 determined by 1H nuclear magnetic resonance.
  Proteins, 37, 388-403.
PDB code: 1bk8
18763132 G.Gao, J.Dai, M.Ding, G.Hellekant, J.Wang, and D.Wang (1999).
Studies on solution NMR structure of brazzein : Secondary structure and molecular scaffold.
  Sci China C Life Sci, 42, 409-419.  
9890560 J.M.Schröder (1999).
Epithelial peptide antibiotics.
  Biochem Pharmacol, 57, 121-134.  
10491073 L.D.Possani, B.Becerril, M.Delepierre, and J.Tytgat (1999).
Scorpion toxins specific for Na+-channels.
  Eur J Biochem, 264, 287-300.  
9715910 C.Bloch, S.U.Patel, F.Baud, M.J.Zvelebil, M.D.Carr, P.J.Sadler, and J.M.Thornton (1998).
1H NMR structure of an antifungal gamma-thionin protein SIalpha1: similarity to scorpion toxins.
  Proteins, 32, 334-349.  
9692330 C.Vita, J.Vizzavona, E.Drakopoulou, S.Zinn-Justin, B.Gilquin, and A.Ménez (1998).
Novel miniproteins engineered by the transfer of active sites to small natural scaffolds.
  Biopolymers, 47, 93.  
9477955 E.Drakopoulou, J.Vizzavona, J.Neyton, V.Aniort, F.Bouet, H.Virelizier, A.Ménez, and C.Vita (1998).
Consequence of the removal of evolutionary conserved disulfide bridges on the structure and function of charybdotoxin and evidence that particular cysteine spacings govern specific disulfide bond formation.
  Biochemistry, 37, 1292-1301.  
10333739 F.García-Olmedo, A.Molina, J.M.Alamillo, and P.Rodríguez-Palenzuéla (1998).
Plant defense peptides.
  Biopolymers, 47, 479-491.  
9628478 J.E.Caldwell, F.Abildgaard, Z.Dzakula, D.Ming, G.Hellekant, and J.L.Markley (1998).
Solution structure of the thermostable sweet-tasting protein brazzein.
  Nat Struct Biol, 5, 427-431.
PDB codes: 1brz 2brz
10333738 J.L.Dimarcq, P.Bulet, C.Hetru, and J.Hoffmann (1998).
Cysteine-rich antimicrobial peptides in invertebrates.
  Biopolymers, 47, 465-477.  
9487696 L.Cavallarin, D.Andreu, and B.San Segundo (1998).
Cecropin A-derived peptides are potent inhibitors of fungal plant pathogens.
  Mol Plant Microbe Interact, 11, 218-227.  
9487736 R.E.Hancock, and R.Lehrer (1998).
Cationic peptides: a new source of antibiotics.
  Trends Biotechnol, 16, 82-88.  
9627406 Y.Nakagawa, M.Sadilek, E.Lehmberg, R.Herrmann, R.Herrmann, H.Moskowitz, Y.M.Lee, B.A.Thomas, R.Shimizu, M.Kuroda, A.D.Jones, and B.D.Hammock (1998).
Rapid purification and molecular modeling of AaIT peptides from venom of Androctonus australis.
  Arch Insect Biochem Physiol, 38, 53-65.  
9223182 C.Landon, P.Sodano, B.Cornet, J.M.Bonmatin, C.Kopeyan, H.Rochat, F.Vovelle, and M.Ptak (1997).
Refined solution structure of the anti-mammal and anti-insect LqqIII scorpion toxin: comparison with other scorpion toxins.
  Proteins, 28, 360-374.  
  9300487 C.Landon, P.Sodano, C.Hetru, J.Hoffmann, and M.Ptak (1997).
Solution structure of drosomycin, the first inducible antifungal protein from insects.
  Protein Sci, 6, 1878-1884.
PDB code: 1myn
9210487 E.Adjadj, V.Naudat, E.Quiniou, D.Wouters, P.Sautière, and C.T.Craescu (1997).
Solution structure of Lqh-8/6, a toxin-like peptide from a scorpion venom--structural heterogeneity induced by proline cis/trans isomerization.
  Eur J Biochem, 246, 218-227.  
8995418 G.W.De Samblanx, I.J.Goderis, K.Thevissen, R.Raemaekers, F.Fant, F.Borremans, D.P.Acland, R.W.Osborn, S.Patel, and W.F.Broekaert (1997).
Mutational analysis of a plant defensin from radish (Raphanus sativus L.) reveals two adjacent sites important for antifungal activity.
  J Biol Chem, 272, 1171-1179.  
9092804 J.Song, B.Gilquin, N.Jamin, E.Drakopoulou, M.Guenneugues, M.Dauplais, C.Vita, and A.Ménez (1997).
NMR solution structure of a two-disulfide derivative of charybdotoxin: structural evidence for conservation of scorpion toxin alpha/beta motif and its hydrophobic side chain packing.
  Biochemistry, 36, 3760-3766.
PDB code: 1bah
9103978 Y.Zhang, and K.Lewis (1997).
Fabatins: new antimicrobial plant peptides.
  FEMS Microbiol Lett, 149, 59-64.  
8973638 B.Selisko, C.Garcia, B.Becerril, M.Delepierre, and L.D.Possani (1996).
An insect-specific toxin from Centruroides noxius Hoffmann. cDNA, primary structure, three-dimensional model and electrostatic surface potentials in comparison with other toxin variants.
  Eur J Biochem, 242, 235-242.  
8612608 C.Landon, B.Cornet, J.M.Bonmatin, C.Kopeyan, H.Rochat, F.Vovelle, and M.Ptak (1996).
1H-NMR-derived secondary structure and the overall fold of the potent anti-mammal and anti-insect toxin III from the scorpion Leiurus quinquestriatus quinquestriatus.
  Eur J Biochem, 236, 395-404.
PDB code: 1lqq
8662609 E.Drakopoulou, S.Zinn-Justin, M.Guenneugues, B.Gilqin, A.Ménez, and C.Vita (1996).
Changing the structural context of a functional beta-hairpin. Synthesis and characterization of a chimera containing the curaremimetic loop of a snake toxin in the scorpion alpha/beta scaffold.
  J Biol Chem, 271, 11979-11987.  
8706720 E.Méndez, A.Rocher, M.Calero, T.Girbés, L.Citores, and F.Soriano (1996).
Primary structure of omega-hordothionin, a member of a novel family of thionins from barley endosperm, and its inhibition of protein synthesis in eukaryotic and prokaryotic cell-free systems.
  Eur J Biochem, 239, 67-73.  
8688418 J.M.Hill, P.F.Alewood, and D.J.Craik (1996).
Three-dimensional solution structure of mu-conotoxin GIIIB, a specific blocker of skeletal muscle sodium channels.
  Biochemistry, 35, 8824-8835.
PDB code: 1gib
8663029 K.Thevissen, A.Ghazi, G.W.De Samblanx, C.Brownlee, R.W.Osborn, and W.F.Broekaert (1996).
Fungal membrane responses induced by plant defensins and thionins.
  J Biol Chem, 271, 15018-15025.  
8785364 L.Moroder, D.Besse, H.J.Musiol, S.Rudolph-Böhner, and F.Siedler (1996).
Oxidative folding of cystine-rich peptides vs regioselective cysteine pairing strategies.
  Biopolymers, 40, 207-234.  
8993365 R.I.Lehrer, and T.Ganz (1996).
Endogenous vertebrate antibiotics. Defensins, protegrins, and other cysteine-rich antimicrobial peptides.
  Ann N Y Acad Sci, 797, 228-239.  
8679614 S.Zinn-Justin, M.Guenneugues, E.Drakopoulou, B.Gilquin, C.Vita, and A.Ménez (1996).
Transfer of a beta-hairpin from the functional site of snake curaremimetic toxins to the alpha/beta scaffold of scorpion toxins: three-dimensional solution structure of the chimeric protein.
  Biochemistry, 35, 8535-8543.
PDB code: 1cmr
7541540 C.Vita, C.Roumestand, F.Toma, and A.Ménez (1995).
Scorpion toxins as natural scaffolds for protein engineering.
  Proc Natl Acad Sci U S A, 92, 6404-6408.  
7705336 G.Nitti, S.Orrù, C.Bloch, L.Morhy, G.Marino, and P.Pucci (1995).
Amino acid sequence and disulphide-bridge pattern of three gamma-thionins from Sorghum bicolor.
  Eur J Biochem, 228, 250-256.  
8555422 M.Bruix, C.González, J.Santoro, F.Soriano, A.Rocher, E.Méndez, and M.Rico (1995).
1H-nmr studies on the structure of a new thionin from barley endosperm.
  Biopolymers, 36, 751-763.  
8055934 M.F.Martin-Eauclaire, M.Søgaard, C.Ramos, S.Cestèle, P.E.Bougis, and B.Svensson (1994).
Production of active, insect-specific scorpion neurotoxin in yeast.
  Eur J Biochem, 223, 637-645.  
  7849598 P.K.Pallaghy, K.J.Nielsen, D.J.Craik, and R.S.Norton (1994).
A common structural motif incorporating a cystine knot and a triple-stranded beta-sheet in toxic and inhibitory polypeptides.
  Protein Sci, 3, 1833-1839.  
8307039 W.Lee, C.H.Moore, D.D.Watt, and N.R.Krishna (1994).
Solution structure of the variant-3 neurotoxin from Centruroides sculpturatus Ewing.
  Eur J Biochem, 219, 89-95.  
15335677 J.F.Bazan (1993).
Emerging families of cytokines and receptors.
  Curr Biol, 3, 603-606.  
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 code is shown on the right.

 

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