PhytophthoraV1, Main, Exploration, bibRecord, 002958

The NMR solution structure and characterization of pH dependent chemical shifts of the beta-elicitin, cryptogein.

Identifieur interne : 002958 ( Main/Exploration ); précédent : 002957; suivant : 002959

The NMR solution structure and characterization of pH dependent chemical shifts of the beta-elicitin, cryptogein.

Auteurs : P R Gooley [Australie] ; M A Keniry ; R A Dimitrov ; D E Marsh ; D W Keizer ; K R Gayler ; B R Grant

Source :

Journal of biomolecular NMR [ 0925-2738 ] ; 1998.

RBID : pubmed:9862128

Descripteurs français

English descriptors

KwdEn :
- Algal Proteins (MeSH), Amino Acid Sequence (MeSH), Carbon Isotopes (MeSH), Crystallography, X-Ray (methods), Fungal Proteins (chemistry), Hydrogen Bonding (MeSH), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Macromolecular Substances (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Nitrogen Isotopes (MeSH), Nuclear Magnetic Resonance, Biomolecular (methods), Protein Structure, Secondary (MeSH).
MESH :
- chemical , chemistry : Fungal Proteins.
- chemical : Algal Proteins, Carbon Isotopes, Macromolecular Substances, Nitrogen Isotopes.
- methods : Crystallography, X-Ray, Nuclear Magnetic Resonance, Biomolecular.
- Amino Acid Sequence, Hydrogen Bonding, Hydrogen-Ion Concentration, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Structure, Secondary.

Abstract

The NMR structure of the 98 residue beta-elicitin, cryptogein, which induces a defence response in tobacco, was determined using 15N and 13C/15N labelled protein samples. In aqueous solution conditions in the millimolar range, the protein forms a discrete homodimer where the N-terminal helices of each monomer form an interface. The structure was calculated with 1047 intrasubunit and 40 intersubunit NOE derived distance constraints and 236 dihedral angle constraints for each subunit using the molecular dynamics program DYANA. The twenty best conformers were energy-minimized in OPAL to give a root-mean-square deviation to the mean structure of 0.82 A for the backbone atoms and 1.03 A for all heavy atoms. The monomeric structure is nearly identical to the recently derived X-ray crystal structure (backbone rmsd 0.86 A for residues 2 to 97) and shows five helices, a two stranded antiparallel beta-sheet and an omega-loop. Using 1H,15N HSQC spectroscopy the pKa of the N- and C-termini, Tyr12, Asp21, Asp30, Asp72, and Tyr85 were determined and support the proposal of several stabilizing ionic interactions including a salt bridge between Asp21 and Lys62. The hydroxyl hydrogens of Tyr33 and Ser78 are clearly observed indicating that these residues are buried and hydrogen bonded. Two other tyrosines, Tyr47 and Tyr87, show pKa's > 12, however, there is no indication that their hydroxyls are hydrogen bonded. Calculations of theoretical pKa's show general agreement with the experimentally determined values and are similar for both the crystal and solution structures.

DOI: 10.1023/a:1008395001008
PubMed: 9862128

Affiliations:

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Le document en format XML

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<term>Amino Acid Sequence (MeSH)</term>
<term>Carbon Isotopes (MeSH)</term>
<term>Crystallography, X-Ray (methods)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Hydrogen Bonding (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Macromolecular Substances (MeSH)</term>
<term>Models, Molecular (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Nitrogen Isotopes (MeSH)</term>
<term>Nuclear Magnetic Resonance, Biomolecular (methods)</term>
<term>Protein Structure, Secondary (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Cinétique (MeSH)</term>
<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Cristallographie aux rayons X (méthodes)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Isotopes de l'azote (MeSH)</term>
<term>Isotopes du carbone (MeSH)</term>
<term>Liaison hydrogène (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Protéines d'algue (MeSH)</term>
<term>Protéines fongiques (composition chimique)</term>
<term>Résonance magnétique nucléaire biomoléculaire (méthodes)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Structures macromoléculaires (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Fungal Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Algal Proteins</term>
<term>Carbon Isotopes</term>
<term>Macromolecular Substances</term>
<term>Nitrogen Isotopes</term>
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<term>Nuclear Magnetic Resonance, Biomolecular</term>
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<keywords scheme="MESH" qualifier="méthodes" xml:lang="fr"><term>Cristallographie aux rayons X</term>
<term>Résonance magnétique nucléaire biomoléculaire</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Hydrogen Bonding</term>
<term>Hydrogen-Ion Concentration</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Structure, Secondary</term>
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<term>Concentration en ions d'hydrogène</term>
<term>Données de séquences moléculaires</term>
<term>Isotopes de l'azote</term>
<term>Isotopes du carbone</term>
<term>Liaison hydrogène</term>
<term>Modèles moléculaires</term>
<term>Protéines d'algue</term>
<term>Structure secondaire des protéines</term>
<term>Structures macromoléculaires</term>
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<front><div type="abstract" xml:lang="en">The NMR structure of the 98 residue beta-elicitin, cryptogein, which induces a defence response in tobacco, was determined using 15N and 13C/15N labelled protein samples. In aqueous solution conditions in the millimolar range, the protein forms a discrete homodimer where the N-terminal helices of each monomer form an interface. The structure was calculated with 1047 intrasubunit and 40 intersubunit NOE derived distance constraints and 236 dihedral angle constraints for each subunit using the molecular dynamics program DYANA. The twenty best conformers were energy-minimized in OPAL to give a root-mean-square deviation to the mean structure of 0.82 A for the backbone atoms and 1.03 A for all heavy atoms. The monomeric structure is nearly identical to the recently derived X-ray crystal structure (backbone rmsd 0.86 A for residues 2 to 97) and shows five helices, a two stranded antiparallel beta-sheet and an omega-loop. Using 1H,15N HSQC spectroscopy the pKa of the N- and C-termini, Tyr12, Asp21, Asp30, Asp72, and Tyr85 were determined and support the proposal of several stabilizing ionic interactions including a salt bridge between Asp21 and Lys62. The hydroxyl hydrogens of Tyr33 and Ser78 are clearly observed indicating that these residues are buried and hydrogen bonded. Two other tyrosines, Tyr47 and Tyr87, show pKa's > 12, however, there is no indication that their hydroxyls are hydrogen bonded. Calculations of theoretical pKa's show general agreement with the experimentally determined values and are similar for both the crystal and solution structures.</div>
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<Abstract><AbstractText>The NMR structure of the 98 residue beta-elicitin, cryptogein, which induces a defence response in tobacco, was determined using 15N and 13C/15N labelled protein samples. In aqueous solution conditions in the millimolar range, the protein forms a discrete homodimer where the N-terminal helices of each monomer form an interface. The structure was calculated with 1047 intrasubunit and 40 intersubunit NOE derived distance constraints and 236 dihedral angle constraints for each subunit using the molecular dynamics program DYANA. The twenty best conformers were energy-minimized in OPAL to give a root-mean-square deviation to the mean structure of 0.82 A for the backbone atoms and 1.03 A for all heavy atoms. The monomeric structure is nearly identical to the recently derived X-ray crystal structure (backbone rmsd 0.86 A for residues 2 to 97) and shows five helices, a two stranded antiparallel beta-sheet and an omega-loop. Using 1H,15N HSQC spectroscopy the pKa of the N- and C-termini, Tyr12, Asp21, Asp30, Asp72, and Tyr85 were determined and support the proposal of several stabilizing ionic interactions including a salt bridge between Asp21 and Lys62. The hydroxyl hydrogens of Tyr33 and Ser78 are clearly observed indicating that these residues are buried and hydrogen bonded. Two other tyrosines, Tyr47 and Tyr87, show pKa's > 12, however, there is no indication that their hydroxyls are hydrogen bonded. Calculations of theoretical pKa's show general agreement with the experimentally determined values and are similar for both the crystal and solution structures.</AbstractText>
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   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:9862128
   |texte=   The NMR solution structure and characterization of pH dependent chemical shifts of the beta-elicitin, cryptogein.
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The NMR solution structure and characterization of pH dependent chemical shifts of the beta-elicitin, cryptogein.

The NMR solution structure and characterization of pH dependent chemical shifts of the beta-elicitin, cryptogein.

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