Structural flexibility of the pentameric SARS coronavirus envelope protein ion channel.
Identifieur interne : 003006 ( Main/Exploration ); précédent : 003005; suivant : 003007Structural flexibility of the pentameric SARS coronavirus envelope protein ion channel.
Auteurs : Krupakar Parthasarathy ; Lifang Ng ; Xin Lin ; Ding Xiang Liu ; Konstantin Pervushin ; Xiandi Gong ; Jaume TorresSource :
- Biophysical journal [ 1542-0086 ] ; 2008.
Descripteurs français
- KwdFr :
- Animaux, Canaux ioniques (), Canaux ioniques (génétique), Canaux ioniques (métabolisme), Caprylates (), Données de séquences moléculaires, Fluorocarbones (), Humains, Modèles moléculaires, Mutation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Souris, Structure tertiaire des protéines, Séquence d'acides aminés, Virus du SRAS (), Électrophorèse.
- MESH :
- génétique : Canaux ioniques, Protéines de l'enveloppe virale.
- métabolisme : Canaux ioniques, Protéines de l'enveloppe virale.
- Animaux, Canaux ioniques, Caprylates, Données de séquences moléculaires, Fluorocarbones, Humains, Modèles moléculaires, Mutation, Protéines de l'enveloppe virale, Souris, Structure tertiaire des protéines, Séquence d'acides aminés, Virus du SRAS, Électrophorèse.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Caprylates (chemistry), Electrophoresis, Fluorocarbons (chemistry), Humans, Ion Channels (chemistry), Ion Channels (genetics), Ion Channels (metabolism), Mice, Models, Molecular, Molecular Sequence Data, Mutation, Protein Structure, Tertiary, SARS Virus (chemistry), Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Caprylates, Fluorocarbons, Ion Channels, Viral Envelope Proteins.
- chemical , genetics : Ion Channels, Viral Envelope Proteins.
- chemical , metabolism : Ion Channels, Viral Envelope Proteins.
- chemistry : SARS Virus.
- Amino Acid Sequence, Animals, Electrophoresis, Humans, Mice, Models, Molecular, Molecular Sequence Data, Mutation, Protein Structure, Tertiary.
Abstract
Coronaviruses contain a small envelope membrane protein with cation-selective ion channel activity mediated by its transmembrane domain (ETM). In a computational study, we proposed that ion channel activity can be explained by either of two similar ETM homopentameric transmembrane alpha-helical bundles, related by a approximately 50 degrees rotation of the helices. Later, we tested this prediction, using site-specific infrared dichroism of a lysine-flanked isotopically labeled ETM peptide from the virus responsible for the severe acute respiratory syndrome, SARS, reconstituted in lipid bilayers. However, the data were consistent with the presence of a kink at the center of the ETM alpha-helix, and it did not fit completely either computational model. Herein, we have used native ETM, without flanking lysines, and show that the helix orientation is now consistent with one of the predicted models. ETM only produced one oligomeric form, pentamers, in the lipid-mimic detergent dodecylphosphocholine and in perfluorooctanoic acid. We thus report the correct backbone model for the pentameric alpha-helical bundle of ETM. The disruptive effects caused by terminal lysines probably highlight the conformational flexibility required during ion channel function.
DOI: 10.1529/biophysj.108.133041
PubMed: 18658207
Affiliations:
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Le document en format XML
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last="Pervushin">Konstantin Pervushin</name></author><author><name sortKey="Gong, Xiandi" sort="Gong, Xiandi" uniqKey="Gong X" first="Xiandi" last="Gong">Xiandi Gong</name></author><author><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></author></analytic><series><title level="j">Biophysical journal</title><idno type="eISSN">1542-0086</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Caprylates (chemistry)</term><term>Electrophoresis</term><term>Fluorocarbons (chemistry)</term><term>Humans</term><term>Ion Channels (chemistry)</term><term>Ion Channels (genetics)</term><term>Ion Channels (metabolism)</term><term>Mice</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux</term><term>Canaux ioniques ()</term><term>Canaux ioniques (génétique)</term><term>Canaux ioniques (métabolisme)</term><term>Caprylates ()</term><term>Données de séquences moléculaires</term><term>Fluorocarbones ()</term><term>Humains</term><term>Modèles moléculaires</term><term>Mutation</term><term>Protéines de l'enveloppe virale ()</term><term>Protéines de l'enveloppe virale (génétique)</term><term>Protéines de l'enveloppe virale (métabolisme)</term><term>Souris</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS ()</term><term>Électrophorèse</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Caprylates</term><term>Fluorocarbons</term><term>Ion Channels</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Ion Channels</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Ion Channels</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Canaux ioniques</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Canaux ioniques</term><term>Protéines de l'enveloppe virale</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Electrophoresis</term><term>Humans</term><term>Mice</term><term>Models, Molecular</term><term>Molecular Sequence Data</term><term>Mutation</term><term>Protein Structure, Tertiary</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Canaux ioniques</term><term>Caprylates</term><term>Données de séquences moléculaires</term><term>Fluorocarbones</term><term>Humains</term><term>Modèles moléculaires</term><term>Mutation</term><term>Protéines de l'enveloppe virale</term><term>Souris</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Virus du SRAS</term><term>Électrophorèse</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses contain a small envelope membrane protein with cation-selective ion channel activity mediated by its transmembrane domain (ETM). In a computational study, we proposed that ion channel activity can be explained by either of two similar ETM homopentameric transmembrane alpha-helical bundles, related by a approximately 50 degrees rotation of the helices. Later, we tested this prediction, using site-specific infrared dichroism of a lysine-flanked isotopically labeled ETM peptide from the virus responsible for the severe acute respiratory syndrome, SARS, reconstituted in lipid bilayers. However, the data were consistent with the presence of a kink at the center of the ETM alpha-helix, and it did not fit completely either computational model. Herein, we have used native ETM, without flanking lysines, and show that the helix orientation is now consistent with one of the predicted models. ETM only produced one oligomeric form, pentamers, in the lipid-mimic detergent dodecylphosphocholine and in perfluorooctanoic acid. We thus report the correct backbone model for the pentameric alpha-helical bundle of ETM. The disruptive effects caused by terminal lysines probably highlight the conformational flexibility required during ion channel function.</div></front></TEI><affiliations><list></list><tree><noCountry><name sortKey="Gong, Xiandi" sort="Gong, Xiandi" uniqKey="Gong X" first="Xiandi" last="Gong">Xiandi Gong</name><name sortKey="Lin, Xin" sort="Lin, Xin" uniqKey="Lin X" first="Xin" last="Lin">Xin Lin</name><name sortKey="Liu, Ding Xiang" sort="Liu, Ding Xiang" uniqKey="Liu D" first="Ding Xiang" last="Liu">Ding Xiang Liu</name><name sortKey="Ng, Lifang" sort="Ng, Lifang" uniqKey="Ng L" first="Lifang" last="Ng">Lifang Ng</name><name sortKey="Parthasarathy, Krupakar" sort="Parthasarathy, Krupakar" uniqKey="Parthasarathy K" first="Krupakar" last="Parthasarathy">Krupakar Parthasarathy</name><name sortKey="Pervushin, Konstantin" sort="Pervushin, Konstantin" uniqKey="Pervushin K" first="Konstantin" last="Pervushin">Konstantin Pervushin</name><name sortKey="Torres, Jaume" sort="Torres, Jaume" uniqKey="Torres J" first="Jaume" last="Torres">Jaume Torres</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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