The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor
Identifieur interne : 002184 ( Main/Merge ); précédent : 002183; suivant : 002185The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor
Auteurs : M. Antonietta Ciardiello [Italie] ; Rossana D'Avino [Italie] ; Angela Amoresano [Italie] ; Lisa Tuppo [Italie] ; Andrea Carpentieri [Italie] ; Vito Carratore [Italie] ; Maurizio Tamburrini [Italie] ; Alfonso Giovane [Italie] ; Piero Pucci [Italie] ; Laura Camardella [Italie]Source :
- Proteins: Structure, Function, and Bioinformatics [ 0887-3585 ] ; 2008-04.
English descriptors
- KwdEn :
Abstract
Pectin methylesterase (PME) from kiwi fruit (Actinidia deliciosa) is a glycoprotein, showing an apparent molecular mass of 50 kDa upon size exclusion chromatography and SDS‐PAGE. The primary structure, elucidated by direct sequencing of the protein, comprises 321 amino acid residues providing a molecular mass of 35 kDa. The protein has an acetylated Thr residue at the amino terminus and five N‐glycosylation consensus sequences, four of which are actually glycosylated. A careful investigation of the oligosaccharide structures demonstrated that PME glycans belong to complex type oligosaccharides essentially consisting of xylosylated polyfucosylated biantennary structures. Alignment with known mature plant PME sequences indicates that the postulated active site residues are conserved. Kiwi PME activity is inhibited following the interaction with the proteinaceous inhibitor PMEI, isolated from the same source. Gel‐filtration experiments show that kiwi PME/PMEI complex is stable in a large pH range and dissociates only at pH 10.0. Modeling of the interaction with the inhibitor was performed by using the crystal structure of the complex between kiwi PMEI and tomato PME as a template. The model shows that the binding site is the same reported for tomato PME. However, additional salt link interactions are found to connect the external loops of kiwi PME to PMEI. This finding may explain the higher pH stability of the complex formed by the two kiwi proteins respect to that formed by PMEI and tomato PME. Proteins 2008. © 2007 Wiley‐Liss, Inc.
Url:
DOI: 10.1002/prot.21681
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: 001273
- to stream Istex, to step Curation: 001273
- to stream Istex, to step Checkpoint: 000558
Links to Exploration step
ISTEX:AEC0F24553B034D2E1949A78ACA1E412BF12E60ELe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor</title><author><name sortKey="Ciardiello, M Antonietta" sort="Ciardiello, M Antonietta" uniqKey="Ciardiello M" first="M. Antonietta" last="Ciardiello">M. Antonietta Ciardiello</name></author><author><name sortKey="D Avino, Rossana" sort="D Avino, Rossana" uniqKey="D Avino R" first="Rossana" last="D'Avino">Rossana D'Avino</name></author><author><name sortKey="Amoresano, Angela" sort="Amoresano, Angela" uniqKey="Amoresano A" first="Angela" last="Amoresano">Angela Amoresano</name></author><author><name sortKey="Tuppo, Lisa" sort="Tuppo, Lisa" uniqKey="Tuppo L" first="Lisa" last="Tuppo">Lisa Tuppo</name></author><author><name sortKey="Carpentieri, Andrea" sort="Carpentieri, Andrea" uniqKey="Carpentieri A" first="Andrea" last="Carpentieri">Andrea Carpentieri</name></author><author><name sortKey="Carratore, Vito" sort="Carratore, Vito" uniqKey="Carratore V" first="Vito" last="Carratore">Vito Carratore</name></author><author><name sortKey="Tamburrini, Maurizio" sort="Tamburrini, Maurizio" uniqKey="Tamburrini M" first="Maurizio" last="Tamburrini">Maurizio Tamburrini</name></author><author><name sortKey="Giovane, Alfonso" sort="Giovane, Alfonso" uniqKey="Giovane A" first="Alfonso" last="Giovane">Alfonso Giovane</name></author><author><name sortKey="Pucci, Piero" sort="Pucci, Piero" uniqKey="Pucci P" first="Piero" last="Pucci">Piero Pucci</name></author><author><name sortKey="Camardella, Laura" sort="Camardella, Laura" uniqKey="Camardella L" first="Laura" last="Camardella">Laura Camardella</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:AEC0F24553B034D2E1949A78ACA1E412BF12E60E</idno><date when="2008" year="2008">2008</date><idno type="doi">10.1002/prot.21681</idno><idno type="url">https://api.istex.fr/document/AEC0F24553B034D2E1949A78ACA1E412BF12E60E/fulltext/pdf</idno><idno type="wicri:Area/Istex/Corpus">001273</idno><idno type="wicri:Area/Istex/Curation">001273</idno><idno type="wicri:Area/Istex/Checkpoint">000558</idno><idno type="wicri:doubleKey">0887-3585:2008:Ciardiello M:the:peculiar:structural</idno><idno type="wicri:Area/Main/Merge">002184</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor</title><author><name sortKey="Ciardiello, M Antonietta" sort="Ciardiello, M Antonietta" uniqKey="Ciardiello M" first="M. Antonietta" last="Ciardiello">M. Antonietta Ciardiello</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="D Avino, Rossana" sort="D Avino, Rossana" uniqKey="D Avino R" first="Rossana" last="D'Avino">Rossana D'Avino</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Amoresano, Angela" sort="Amoresano, Angela" uniqKey="Amoresano A" first="Angela" last="Amoresano">Angela Amoresano</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Organic Chemistry and Biochemistry, University Federico II of Napoli, 80126 Napoli</wicri:regionArea><wicri:noRegion>80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Tuppo, Lisa" sort="Tuppo, Lisa" uniqKey="Tuppo L" first="Lisa" last="Tuppo">Lisa Tuppo</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Carpentieri, Andrea" sort="Carpentieri, Andrea" uniqKey="Carpentieri A" first="Andrea" last="Carpentieri">Andrea Carpentieri</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Organic Chemistry and Biochemistry, University Federico II of Napoli, 80126 Napoli</wicri:regionArea><wicri:noRegion>80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Carratore, Vito" sort="Carratore, Vito" uniqKey="Carratore V" first="Vito" last="Carratore">Vito Carratore</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Tamburrini, Maurizio" sort="Tamburrini, Maurizio" uniqKey="Tamburrini M" first="Maurizio" last="Tamburrini">Maurizio Tamburrini</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Giovane, Alfonso" sort="Giovane, Alfonso" uniqKey="Giovane A" first="Alfonso" last="Giovane">Alfonso Giovane</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Biochemistry and Biophysics, Second University of Napoli, 80138 Napoli</wicri:regionArea><wicri:noRegion>80138 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Pucci, Piero" sort="Pucci, Piero" uniqKey="Pucci P" first="Piero" last="Pucci">Piero Pucci</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Department of Organic Chemistry and Biochemistry, University Federico II of Napoli, 80126 Napoli</wicri:regionArea><wicri:noRegion>80126 Napoli</wicri:noRegion></affiliation></author><author><name sortKey="Camardella, Laura" sort="Camardella, Laura" uniqKey="Camardella L" first="Laura" last="Camardella">Laura Camardella</name><affiliation wicri:level="1"><country xml:lang="fr">Italie</country><wicri:regionArea>Institute of Protein Biochemistry, C.N.R., 80131 Napoli</wicri:regionArea><wicri:noRegion>80131 Napoli</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Proteins: Structure, Function, and Bioinformatics</title><title level="j" type="abbrev">Proteins</title><idno type="ISSN">0887-3585</idno><idno type="eISSN">1097-0134</idno><imprint><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2008-04">2008-04</date><biblScope unit="volume">71</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="195">195</biblScope><biblScope unit="page" to="206">206</biblScope></imprint><idno type="ISSN">0887-3585</idno></series><idno type="istex">AEC0F24553B034D2E1949A78ACA1E412BF12E60E</idno><idno type="DOI">10.1002/prot.21681</idno><idno type="ArticleID">PROT21681</idno></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0887-3585</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>amino acid sequence</term><term>glycosylation</term><term>kiwi fruit</term><term>modeling</term><term>pectin methylesterase</term><term>pectin methylesterase inhibitor</term><term>protein–protein interaction</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Pectin methylesterase (PME) from kiwi fruit (Actinidia deliciosa) is a glycoprotein, showing an apparent molecular mass of 50 kDa upon size exclusion chromatography and SDS‐PAGE. The primary structure, elucidated by direct sequencing of the protein, comprises 321 amino acid residues providing a molecular mass of 35 kDa. The protein has an acetylated Thr residue at the amino terminus and five N‐glycosylation consensus sequences, four of which are actually glycosylated. A careful investigation of the oligosaccharide structures demonstrated that PME glycans belong to complex type oligosaccharides essentially consisting of xylosylated polyfucosylated biantennary structures. Alignment with known mature plant PME sequences indicates that the postulated active site residues are conserved. Kiwi PME activity is inhibited following the interaction with the proteinaceous inhibitor PMEI, isolated from the same source. Gel‐filtration experiments show that kiwi PME/PMEI complex is stable in a large pH range and dissociates only at pH 10.0. Modeling of the interaction with the inhibitor was performed by using the crystal structure of the complex between kiwi PMEI and tomato PME as a template. The model shows that the binding site is the same reported for tomato PME. However, additional salt link interactions are found to connect the external loops of kiwi PME to PMEI. This finding may explain the higher pH stability of the complex formed by the two kiwi proteins respect to that formed by PMEI and tomato PME. Proteins 2008. © 2007 Wiley‐Liss, Inc.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Bois/explor/OrangerV1/Data/Main/Merge
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002184 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Merge/biblio.hfd -nk 002184 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Wicri/Bois
|area= OrangerV1
|flux= Main
|étape= Merge
|type= RBID
|clé= ISTEX:AEC0F24553B034D2E1949A78ACA1E412BF12E60E
|texte= The peculiar structural features of kiwi fruit pectin methylesterase: Amino acid sequence, oligosaccharides structure, and modeling of the interaction with its natural proteinaceous inhibitor
}}
| This area was generated with Dilib version V0.6.25. |  |