Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.
Identifieur interne : 000069 ( Main/Corpus ); précédent : 000068; suivant : 000070Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.
Auteurs : Tetsuya Masuda ; Satomi Kigo ; Mayuko Mitsumoto ; Keisuke Ohta ; Mamoru Suzuki ; Bunzo Mikami ; Naofumi Kitabatake ; Fumito TaniSource :
- Frontiers in molecular biosciences [ 2296-889X ] ; 2018.
Abstract
Thaumatin, an intensely sweet-tasting protein, elicits sweet taste with a threshold of only 50 nM. Previous studies from our laboratory suggested that the complex model between the T1R2-T1R3 sweet receptor and thaumatin depends critically on the complementarity of electrostatic potentials. In order to further validate this model, we focused on three lysine residues (Lys78, Lys106, and Lys137), which were expected to be part of the interaction sites. Three thaumatin mutants (K78A, K106A, and K137A) were prepared and their threshold values of sweetness were examined. The results showed that the sweetness of K106A was reduced by about three times and those of K78A and K137A were reduced by about five times when compared to wild-type thaumatin. The three-dimensional structures of these mutants were also determined by X-ray crystallographic analyses at atomic resolutions. The overall structures of mutant proteins were similar to that of wild-type but the electrostatic potentials around the mutated sites became more negative. Since the three lysine residues are located in 20-40 Å apart each other on the surface of thaumatin molecule, these results suggest the positive charges on the surface of thaumatin play a crucial role in the interaction with the sweet receptor, and are consistent with a large surface is required for interaction with the sweet receptor, as proposed by the multipoint interaction model named wedge model.
DOI: 10.3389/fmolb.2018.00010
PubMed: 29487853
PubMed Central: PMC5816810
Links to Exploration step
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Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name><affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Suzuki, Mamoru" sort="Suzuki, Mamoru" uniqKey="Suzuki M" first="Mamoru" last="Suzuki">Mamoru Suzuki</name><affiliation><nlm:affiliation>Laboratory of Supramolecular Crystallography, Research Center for State-of-the-Art Functional Protein Analysis, Institute for Protein Research, Osaka University, Suita, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Mikami, Bunzo" sort="Mikami, Bunzo" uniqKey="Mikami B" first="Bunzo" last="Mikami">Bunzo Mikami</name><affiliation><nlm:affiliation>Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name><affiliation><nlm:affiliation>Department of Foods and Human Nutrition, Notre Dame Seishin University, Okayama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Tani, Fumito" sort="Tani, Fumito" uniqKey="Tani F" first="Fumito" last="Tani">Fumito Tani</name><affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29487853</idno><idno type="pmid">29487853</idno><idno type="doi">10.3389/fmolb.2018.00010</idno><idno type="pmc">PMC5816810</idno><idno type="wicri:Area/Main/Corpus">000069</idno><idno 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last="Mitsumoto">Mayuko Mitsumoto</name><affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Ohta, Keisuke" sort="Ohta, Keisuke" uniqKey="Ohta K" first="Keisuke" last="Ohta">Keisuke Ohta</name><affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Suzuki, Mamoru" sort="Suzuki, Mamoru" uniqKey="Suzuki M" first="Mamoru" last="Suzuki">Mamoru Suzuki</name><affiliation><nlm:affiliation>Laboratory of Supramolecular Crystallography, Research Center for State-of-the-Art Functional Protein Analysis, Institute for Protein Research, Osaka University, Suita, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Mikami, Bunzo" sort="Mikami, Bunzo" uniqKey="Mikami B" first="Bunzo" last="Mikami">Bunzo Mikami</name><affiliation><nlm:affiliation>Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Kitabatake, Naofumi" sort="Kitabatake, Naofumi" uniqKey="Kitabatake N" first="Naofumi" last="Kitabatake">Naofumi Kitabatake</name><affiliation><nlm:affiliation>Department of Foods and Human Nutrition, Notre Dame Seishin University, Okayama, Japan.</nlm:affiliation></affiliation></author><author><name sortKey="Tani, Fumito" sort="Tani, Fumito" uniqKey="Tani F" first="Fumito" last="Tani">Fumito Tani</name><affiliation><nlm:affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Frontiers in molecular biosciences</title><idno type="ISSN">2296-889X</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thaumatin, an intensely sweet-tasting protein, elicits sweet taste with a threshold of only 50 nM. Previous studies from our laboratory suggested that the complex model between the T1R2-T1R3 sweet receptor and thaumatin depends critically on the complementarity of electrostatic potentials. In order to further validate this model, we focused on three lysine residues (Lys78, Lys106, and Lys137), which were expected to be part of the interaction sites. Three thaumatin mutants (K78A, K106A, and K137A) were prepared and their threshold values of sweetness were examined. The results showed that the sweetness of K106A was reduced by about three times and those of K78A and K137A were reduced by about five times when compared to wild-type thaumatin. The three-dimensional structures of these mutants were also determined by X-ray crystallographic analyses at atomic resolutions. The overall structures of mutant proteins were similar to that of wild-type but the electrostatic potentials around the mutated sites became more negative. Since the three lysine residues are located in 20-40 Å apart each other on the surface of thaumatin molecule, these results suggest the positive charges on the surface of thaumatin play a crucial role in the interaction with the sweet receptor, and are consistent with a large surface is required for interaction with the sweet receptor, as proposed by the multipoint interaction model named wedge model.</div></front></TEI><pubmed><MedlineCitation Status="PubMed-not-MEDLINE" Owner="NLM"><PMID Version="1">29487853</PMID><DateRevised><Year>2020</Year><Month>09</Month><Day>30</Day></DateRevised><Article PubModel="Electronic-eCollection"><Journal><ISSN IssnType="Print">2296-889X</ISSN><JournalIssue CitedMedium="Print"><Volume>5</Volume><PubDate><Year>2018</Year></PubDate></JournalIssue><Title>Frontiers in molecular biosciences</Title><ISOAbbreviation>Front Mol Biosci</ISOAbbreviation></Journal><ArticleTitle>Positive Charges on the Surface of Thaumatin Are Crucial for the Multi-Point Interaction with the Sweet Receptor.</ArticleTitle><Pagination><MedlinePgn>10</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.3389/fmolb.2018.00010</ELocationID><Abstract><AbstractText>Thaumatin, an intensely sweet-tasting protein, elicits sweet taste with a threshold of only 50 nM. Previous studies from our laboratory suggested that the complex model between the T1R2-T1R3 sweet receptor and thaumatin depends critically on the complementarity of electrostatic potentials. In order to further validate this model, we focused on three lysine residues (Lys78, Lys106, and Lys137), which were expected to be part of the interaction sites. Three thaumatin mutants (K78A, K106A, and K137A) were prepared and their threshold values of sweetness were examined. The results showed that the sweetness of K106A was reduced by about three times and those of K78A and K137A were reduced by about five times when compared to wild-type thaumatin. The three-dimensional structures of these mutants were also determined by X-ray crystallographic analyses at atomic resolutions. The overall structures of mutant proteins were similar to that of wild-type but the electrostatic potentials around the mutated sites became more negative. Since the three lysine residues are located in 20-40 Å apart each other on the surface of thaumatin molecule, these results suggest the positive charges on the surface of thaumatin play a crucial role in the interaction with the sweet receptor, and are consistent with a large surface is required for interaction with the sweet receptor, as proposed by the multipoint interaction model named wedge model.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Masuda</LastName><ForeName>Tetsuya</ForeName><Initials>T</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kigo</LastName><ForeName>Satomi</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mitsumoto</LastName><ForeName>Mayuko</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Ohta</LastName><ForeName>Keisuke</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Suzuki</LastName><ForeName>Mamoru</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Laboratory of Supramolecular Crystallography, Research Center for State-of-the-Art Functional Protein Analysis, Institute for Protein Research, Osaka University, Suita, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Mikami</LastName><ForeName>Bunzo</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kitabatake</LastName><ForeName>Naofumi</ForeName><Initials>N</Initials><AffiliationInfo><Affiliation>Department of Foods and Human Nutrition, Notre Dame Seishin University, Okayama, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Tani</LastName><ForeName>Fumito</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Division of Food Science and Biotechnology, Graduate School of Agriculture, Kyoto University, Uji, Japan.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate 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