PoplarV1, Main, Exploration, bibRecord, 004A31

Sequence replacements in the central beta-turn of plastocyanin.

Identifieur interne : 004A31 ( Main/Exploration ); précédent : 004A30; suivant : 004A32

Sequence replacements in the central beta-turn of plastocyanin.

Auteurs : J A Ybe [États-Unis] ; M H Hecht

Source :

Protein science : a publication of the Protein Society [ 0961-8368 ] ; 1996.

RBID : pubmed:8732753

Descripteurs français

KwdFr :
- Banque de gènes (MeSH), Colorimétrie (MeSH), Cuivre (analyse), Dichroïsme circulaire (MeSH), Données de séquences moléculaires (MeSH), Dénaturation des protéines (MeSH), Escherichia coli (génétique), Gènes de synthèse (MeSH), Modèles moléculaires (MeSH), Mutagenèse dirigée (MeSH), Méthode de Monte Carlo (MeSH), Plastocyanine (composition chimique), Plastocyanine (génétique), Pliage des protéines (MeSH), Protéines de fusion recombinantes (composition chimique), Structure secondaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Séquence nucléotidique (MeSH).
MESH :
- analyse : Cuivre.
- composition chimique : Plastocyanine, Protéines de fusion recombinantes.
- génétique : Escherichia coli, Plastocyanine.
- Banque de gènes, Colorimétrie, Dichroïsme circulaire, Données de séquences moléculaires, Dénaturation des protéines, Gènes de synthèse, Modèles moléculaires, Mutagenèse dirigée, Méthode de Monte Carlo, Pliage des protéines, Structure secondaire des protéines, Séquence d'acides aminés, Séquence nucléotidique.

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Base Sequence (MeSH), Circular Dichroism (MeSH), Colorimetry (MeSH), Copper (analysis), Escherichia coli (genetics), Gene Library (MeSH), Genes, Synthetic (MeSH), Models, Molecular (MeSH), Molecular Sequence Data (MeSH), Monte Carlo Method (MeSH), Mutagenesis, Site-Directed (MeSH), Plastocyanin (chemistry), Plastocyanin (genetics), Protein Denaturation (MeSH), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Recombinant Fusion Proteins (chemistry).
MESH :
- chemical , analysis : Copper.
- chemical , chemistry : Plastocyanin, Recombinant Fusion Proteins.
- genetics : Escherichia coli, Plastocyanin.
- Amino Acid Sequence, Base Sequence, Circular Dichroism, Colorimetry, Gene Library, Genes, Synthetic, Models, Molecular, Molecular Sequence Data, Monte Carlo Method, Mutagenesis, Site-Directed, Protein Denaturation, Protein Folding, Protein Structure, Secondary.

Abstract

The role of beta-turns in dictating the structure of a beta-barrel protein is assessed by probing the tolerance of the central beta-turn of poplar plastocyanin to substitution by arbitrary sequences. Native plastocyanin binds copper and is colored bright blue. However, when the wild-type Pro47-Ser48-Gly49-Val50 turn sequence is replaced by arbitrary tetrapeptides, the vast majority (92/98 = 94%) of mutant proteins cannot fold into the native blue structure. Characterization of the colorless mutant proteins demonstrates that the majority of substitutions in this type II beta-turn disrupt the native structure severely. Gross structural changes are indicated by major differences in the CD spectra of the mutants relative to the wild-type protein, and by the much larger apparent size of mutant proteins in gel filtration experiments. These mutant proteins do not bind copper. Furthermore, Cys84 forms a disulfide bond readily in the colorless mutant proteins, indicating that it has moved away from the buried position it occupies in the native copper binding site and has become exposed. These results indicate that the central beta-turn in plastocyanin is not merely a default structure arising in response to the surrounding context; rather, sequence information in this turn plays an active role in dictating the location of a chain reversal in the beta-barrel structure. These findings are discussed in terms of their implications for the folding of natural proteins, as well as the design of de novo proteins.

DOI: 10.1002/pro.5560050503
PubMed: 8732753
PubMed Central: PMC2143404

Affiliations:

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Le document en format XML

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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>Circular Dichroism (MeSH)</term>
<term>Colorimetry (MeSH)</term>
<term>Copper (analysis)</term>
<term>Escherichia coli (genetics)</term>
<term>Gene Library (MeSH)</term>
<term>Genes, Synthetic (MeSH)</term>
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<term>Molecular Sequence Data (MeSH)</term>
<term>Monte Carlo Method (MeSH)</term>
<term>Mutagenesis, Site-Directed (MeSH)</term>
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<term>Plastocyanin (genetics)</term>
<term>Protein Denaturation (MeSH)</term>
<term>Protein Folding (MeSH)</term>
<term>Protein Structure, Secondary (MeSH)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Banque de gènes (MeSH)</term>
<term>Colorimétrie (MeSH)</term>
<term>Cuivre (analyse)</term>
<term>Dichroïsme circulaire (MeSH)</term>
<term>Données de séquences moléculaires (MeSH)</term>
<term>Dénaturation des protéines (MeSH)</term>
<term>Escherichia coli (génétique)</term>
<term>Gènes de synthèse (MeSH)</term>
<term>Modèles moléculaires (MeSH)</term>
<term>Mutagenèse dirigée (MeSH)</term>
<term>Méthode de Monte Carlo (MeSH)</term>
<term>Plastocyanine (composition chimique)</term>
<term>Plastocyanine (génétique)</term>
<term>Pliage des protéines (MeSH)</term>
<term>Protéines de fusion recombinantes (composition chimique)</term>
<term>Structure secondaire des protéines (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Séquence nucléotidique (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analysis" xml:lang="en"><term>Copper</term>
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<term>Recombinant Fusion Proteins</term>
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<keywords scheme="MESH" qualifier="analyse" xml:lang="fr"><term>Cuivre</term>
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<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term>
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<term>Models, Molecular</term>
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<term>Monte Carlo Method</term>
<term>Mutagenesis, Site-Directed</term>
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<term>Protein Folding</term>
<term>Protein Structure, Secondary</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Banque de gènes</term>
<term>Colorimétrie</term>
<term>Dichroïsme circulaire</term>
<term>Données de séquences moléculaires</term>
<term>Dénaturation des protéines</term>
<term>Gènes de synthèse</term>
<term>Modèles moléculaires</term>
<term>Mutagenèse dirigée</term>
<term>Méthode de Monte Carlo</term>
<term>Pliage des protéines</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">The role of beta-turns in dictating the structure of a beta-barrel protein is assessed by probing the tolerance of the central beta-turn of poplar plastocyanin to substitution by arbitrary sequences. Native plastocyanin binds copper and is colored bright blue. However, when the wild-type Pro47-Ser48-Gly49-Val50 turn sequence is replaced by arbitrary tetrapeptides, the vast majority (92/98 = 94%) of mutant proteins cannot fold into the native blue structure. Characterization of the colorless mutant proteins demonstrates that the majority of substitutions in this type II beta-turn disrupt the native structure severely. Gross structural changes are indicated by major differences in the CD spectra of the mutants relative to the wild-type protein, and by the much larger apparent size of mutant proteins in gel filtration experiments. These mutant proteins do not bind copper. Furthermore, Cys84 forms a disulfide bond readily in the colorless mutant proteins, indicating that it has moved away from the buried position it occupies in the native copper binding site and has become exposed. These results indicate that the central beta-turn in plastocyanin is not merely a default structure arising in response to the surrounding context; rather, sequence information in this turn plays an active role in dictating the location of a chain reversal in the beta-barrel structure. These findings are discussed in terms of their implications for the folding of natural proteins, as well as the design of de novo proteins.</div>
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<Abstract><AbstractText>The role of beta-turns in dictating the structure of a beta-barrel protein is assessed by probing the tolerance of the central beta-turn of poplar plastocyanin to substitution by arbitrary sequences. Native plastocyanin binds copper and is colored bright blue. However, when the wild-type Pro47-Ser48-Gly49-Val50 turn sequence is replaced by arbitrary tetrapeptides, the vast majority (92/98 = 94%) of mutant proteins cannot fold into the native blue structure. Characterization of the colorless mutant proteins demonstrates that the majority of substitutions in this type II beta-turn disrupt the native structure severely. Gross structural changes are indicated by major differences in the CD spectra of the mutants relative to the wild-type protein, and by the much larger apparent size of mutant proteins in gel filtration experiments. These mutant proteins do not bind copper. Furthermore, Cys84 forms a disulfide bond readily in the colorless mutant proteins, indicating that it has moved away from the buried position it occupies in the native copper binding site and has become exposed. These results indicate that the central beta-turn in plastocyanin is not merely a default structure arising in response to the surrounding context; rather, sequence information in this turn plays an active role in dictating the location of a chain reversal in the beta-barrel structure. These findings are discussed in terms of their implications for the folding of natural proteins, as well as the design of de novo proteins.</AbstractText>
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<Reference><Citation>J Mol Biol. 1994 May 20;238(5):733-47</Citation>
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<Reference><Citation>Science. 1993 Dec 10;262(5140):1680-5</Citation>
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   |texte=   Sequence replacements in the central beta-turn of plastocyanin.
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Sequence replacements in the central beta-turn of plastocyanin.

Sequence replacements in the central beta-turn of plastocyanin.

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