Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea, a member of a novel class of plant necrotic proteins

Boissy, Guillaume; Fortelle, Eric de La; Kahn, Richard; Huet, Jean‐Claude; Bricogne, G.; Pernollet, Jean‐Claude; Brunie, Simone

doi:10.1016/s0969-2126(96)00150-5

Cited by 97 publications

(76 citation statements)

References 46 publications

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“…The close correlation found between replacement efficiency and affinity for sterols ( Figure 2B) strongly suggests that cryptogein displacement from its binding sites is secured only by sterol-loaded elicitins. The purified proteins (native state) from both Phytophthora and Pichia culture filtrates are "void," i.e., sterol-unloaded proteins, as it appeared in this work and from structural (Boissy et al, 1996;Fefeu et al, 1997;Gooley et al, 1998) and chemical (Mikes et al, 1997(Mikes et al, , 1998 analyses. It was previously reported that elicitins easily bind sterols from tobacco plasma membranes (Vauthrin et al, 1999).…”

Section: Role Of Sterol-elicitin Complexes In Elicitin Binding To Spementioning

confidence: 52%

“…They are buried inside the core in a highly hydrophobic environment; therefore, Y-F exchange (almost similar steric hindrance but higher hydrophobicity) results in minor changes in the aromatic ring orientations. This was partially demonstrated by circular dichroism, chromatographic, electrophoretic, and spectrophotometric properties (Osman, Vauthrin, Mikes, Milat, Panabières, Marais, Brunie, Maume, Ponchet, and Blein, unpublished results) and was confirmed by the modeling of these mutations in the Swiss-PdbViewer program, with the use of a crystal structure (pdb 1beo; Boissy et al, 1996) and 18 solution structures (pdb 1beg; Fefeu et al, 1997). In fact, the Y-F replacements, after energy minimization, led to small changes in the ring orientation, close to the average position of tyrosine residues revealed by the solution structures.…”

Section: Cryptogein and Mutated Elicitin Characteristicsmentioning

confidence: 78%

“…Permutation of tyrosine-47 and tyrosine-87 with phenylalanine does not change the overall structure of the resulting mutated proteins because the phenolic function of these two tyrosines are free of constraint and do not contribute to protein stability (Boissy et al, 1996;Fefeu et al, 1997;Gooley et al, 1998). They are buried inside the core in a highly hydrophobic environment; therefore, Y-F exchange (almost similar steric hindrance but higher hydrophobicity) results in minor changes in the aromatic ring orientations.…”

Section: Cryptogein and Mutated Elicitin Characteristicsmentioning

confidence: 99%

“…This could be explained by the behavior of this tyrosine residue during complex formation. In the native cryptogein, it stays in the hydrophobic cavity (Boissy et al, 1996;Fefeu et al, 1997;Gooley et al, 1998), whereas in the sterol-loaded cryptogein, it rotates and becomes exposed to solvent (Boissy et al, 1999; Figure 1). The tyrosine residue could be in contact with the aqueous environment, because of its hydrophilic hydroxyl, whereas the hydrophobic phenylalanine residue could not.…”

Section: Involvement Of Tyrosine-47 and -87 In The Sterolelicitin Commentioning

confidence: 99%

“…These amino acids were chosen for their characteristics as highlighted by structural observations (Boissy et al, 1996(Boissy et al, , 1999. Tyrosine-47 residue is involved in the sole hydrogen bond between the protein core and the sterol hydroxyl (Figure 1).…”

Section: Introductionmentioning

confidence: 99%

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Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Osman¹,

Vauthrin²,

Mikeš

et al. 2001

MBoC

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105

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Elicitins secreted by phytopathogenic Phytophthora spp. are proteinaceous elicitors of plant defense mechanisms and were demonstrated to load, carry, and transfer sterols between membranes. The link between elicitor and sterol-loading properties was assessed with the use of site-directed mutagenesis of the 47 and 87 cryptogein tyrosine residues, postulated to be involved in sterol binding. Mutated cryptogeins were tested for their ability to load sterols, bind to plasma membrane putative receptors, and trigger biological responses. For each mutated elicitin, the chemical characterization of the corresponding complexes with stigmasterol (1:1 stoichiometry) demonstrated their full functionality. However, these proteins were strongly altered in their sterol-loading efficiency, specific binding to high-affinity sites, and activities on tobacco cells. Ligand replacement experiments strongly suggest that the formation of a sterol-elicitin complex is a requisite step before elicitins fasten to specific binding sites. This was confirmed with the use of two sterol-preloaded elicitins. Both more rapidly displaced labeled cryptogein from its specific binding sites than the unloaded proteins. Moreover, the binding kinetics of elicitins are related to their biological effects, which constitutes the first evidence that binding sites could be the biological receptors. The first event involved in elicitin-mediated cell responses is proposed to be the protein loading with a sterol molecule.

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Section: Role Of Sterol-elicitin Complexes In Elicitin Binding To Spementioning

confidence: 52%

Section: Cryptogein and Mutated Elicitin Characteristicsmentioning

confidence: 78%

Section: Cryptogein and Mutated Elicitin Characteristicsmentioning

confidence: 99%

Section: Involvement Of Tyrosine-47 and -87 In The Sterolelicitin Commentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 3 more Smart Citations

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Osman¹,

Vauthrin²,

Mikeš

et al. 2001

MBoC

Self Cite

105

View full text Add to dashboard Cite

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Distant homology recognition using structural classification of proteins

Bateman¹

1997

Proteins

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Protein structure prediction is arguably the biggest unsolved problem of structural biology. The notion of the number of naturally occurring different protein folds being limited allows partial solution of this problem by the use of fold recognition methods, which ''thread'' the sequence in question through a library of known protein folds. The fold recognition methods were thought to be superior to the distant homology recognition methods when there is no significant sequence similarity to known structures. We show here that the Structural Classification of Proteins (SCOP) database, organizing all known protein folds according their structural and evolutionary relationships, can be effectively used to enhance the sensitivity of the distant homology recognition methods to rival the ''threading'' methods. In the CASP2 experiment, our approach correctly assigned into existing SCOP superfamilies all of the six ''fold recognition'' targets we attempted. For each of the six targets, we correctly predicted the homologous protein with a very similar structure; often, it was the most similar structure. We correctly predicted local alignments of the sequence features that we found to be characteristic for the protein superfamily containing a given target. Our global alignments, extended manually from these local alignments, also appeared to be rather accurate. Proteins, Suppl. 1:105-112, 1997. 1998 Wiley-Liss, Inc.

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Distant homology recognition using structural classification of proteins

Murzin¹,

Bateman

1997

Proteins

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Protein structure prediction is arguably the biggest unsolved problem of structural biology. The notion of the number of naturally occurring different protein folds being limited allows partial solution of this problem by the use of fold recognition methods, which "thread" the sequence in question through a library of known protein folds. The fold recognition methods were thought to be superior to the distant homology recognition methods when there is no significant sequence similarity to known structures. We show here that the Structural Classification of Proteins (SCOP) database, organizing all known protein folds according their structural and evolutionary relationships, can be effectively used to enhance the sensitivity of the distant homology recognition methods to rival the "threading" methods. In the CASP2 experiment, our approach correctly assigned into existing SCOP superfamilies all of the six "fold recognition" targets we attempted. For each of the six targets, we correctly predicted the homologous protein with a very similar structure; often, it was the most similar structure. We correctly predicted local alignments of the sequence features that we found to be characteristic for the protein superfamily containing a given target. Our global alignments, extended manually from these local alignments, also appeared to be rather accurate.

show abstract

Crystal structure of a fungal elicitor secreted by Phytophthora cryptogea, a member of a novel class of plant necrotic proteins

Cited by 97 publications

References 46 publications

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Mediation of Elicitin Activity on Tobacco Is Assumed by Elicitin-Sterol Complexes

Distant homology recognition using structural classification of proteins

Distant homology recognition using structural classification of proteins

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