Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.
Identifieur interne : 002858 ( Ncbi/Merge ); précédent : 002857; suivant : 002859Structure of a conserved Golgi complex-targeting signal in coronavirus envelope proteins.
Auteurs : Yan Li [Singapour] ; Wahyu Surya ; Stephanie Claudine ; Jaume TorresSource :
- The Journal of biological chemistry [ 1083-351X ] ; 2014.
Descripteurs français
- KwdFr :
- Appareil de Golgi (métabolisme), Dichroïsme circulaire, Données de séquences moléculaires, Escherichia coli (génétique), Humains, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines de l'enveloppe virale (), Protéines de l'enveloppe virale (génétique), Protéines de l'enveloppe virale (métabolisme), Protéines recombinantes (), Protéines recombinantes (métabolisme), Similitude de séquences d'acides aminés, Sites de fixation (génétique), Spectroscopie infrarouge à transformée de Fourier, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Transduction du signal, Virus du SRAS (génétique), Virus du SRAS (métabolisme), Électrophorèse sur gel de polyacrylamide.
- MESH :
- génétique : Escherichia coli, Protéines de l'enveloppe virale, Sites de fixation, Virus du SRAS.
- métabolisme : Appareil de Golgi, Protéines de l'enveloppe virale, Protéines recombinantes, Virus du SRAS.
- Dichroïsme circulaire, Données de séquences moléculaires, Humains, Modèles moléculaires, Multimérisation de protéines, Mutation, Protéines de l'enveloppe virale, Protéines recombinantes, Similitude de séquences d'acides aminés, Spectroscopie infrarouge à transformée de Fourier, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Transduction du signal, Électrophorèse sur gel de polyacrylamide.
English descriptors
- KwdEn :
- Amino Acid Sequence, Binding Sites (genetics), Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Escherichia coli (genetics), Golgi Apparatus (metabolism), Humans, Models, Molecular, Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins (chemistry), Recombinant Proteins (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Sequence Homology, Amino Acid, Signal Transduction, Spectroscopy, Fourier Transform Infrared, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemistry : Recombinant Proteins, Viral Envelope Proteins.
- genetics : Binding Sites, Escherichia coli, SARS Virus, Viral Envelope Proteins.
- metabolism : Golgi Apparatus, Recombinant Proteins, SARS Virus, Viral Envelope Proteins.
- Amino Acid Sequence, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Humans, Models, Molecular, Molecular Sequence Data, Mutation, Protein Multimerization, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Signal Transduction, Spectroscopy, Fourier Transform Infrared.
Abstract
Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations.
DOI: 10.1074/jbc.M114.560094
PubMed: 24668816
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du signal</term><term>Virus du SRAS (génétique)</term><term>Virus du SRAS (métabolisme)</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Recombinant Proteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Binding Sites</term><term>Escherichia coli</term><term>SARS Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Escherichia coli</term><term>Protéines de l'enveloppe virale</term><term>Sites de fixation</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Golgi Apparatus</term><term>Recombinant Proteins</term><term>SARS Virus</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Appareil de Golgi</term><term>Protéines de 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infrarouge à transformée de Fourier</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Transduction du signal</term><term>Électrophorèse sur gel de polyacrylamide</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronavirus envelope (CoV E) proteins are ∼100-residue polypeptides with at least one channel-forming α-helical transmembrane (TM) domain. The extramembrane C-terminal tail contains a completely conserved proline, at the center of a predicted β-coil-β motif. This hydrophobic motif has been reported to constitute a Golgi-targeting signal or a second TM domain. However, no structural data for this or other extramembrane domains in CoV E proteins is available. Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24668816</PMID><DateCompleted><Year>2014</Year><Month>08</Month><Day>02</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1083-351X</ISSN><JournalIssue CitedMedium="Internet"><Volume>289</Volume><Issue>18</Issue><PubDate><Year>2014</Year><Month>May</Month><Day>02</Day></PubDate></JournalIssue><Title>The Journal of biological chemistry</Title><ISOAbbreviation>J. Biol. 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Herein, we show that the E protein in the severe acute respiratory syndrome virus has only one TM domain in micelles, whereas the predicted β-coil-β motif forms a short membrane-bound α-helix connected by a disordered loop to the TM domain. However, complementary results suggest that this motif is potentially poised for conformational change or in dynamic exchange with other conformations. </AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Yan</ForeName><Initials>Y</Initials><AffiliationInfo><Affiliation>From the School of Biological Sciences, Nanyang Technological University, 60 Nanyang Drive, 637551 Singapore.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Surya</LastName><ForeName>Wahyu</ForeName><Initials>W</Initials></Author><Author ValidYN="Y"><LastName>Claudine</LastName><ForeName>Stephanie</ForeName><Initials>S</Initials></Author><Author ValidYN="Y"><LastName>Torres</LastName><ForeName>Jaume</ForeName><Initials>J</Initials></Author></AuthorList><Language>eng</Language><DataBankList 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Analytical Ultracentrifugation</Keyword><Keyword MajorTopicYN="N">Coronavirus</Keyword><Keyword MajorTopicYN="N">Envelope Protein</Keyword><Keyword MajorTopicYN="N">Golgi Targeting</Keyword><Keyword MajorTopicYN="N">Nuclear Magnetic Resonance (NMR)</Keyword><Keyword MajorTopicYN="N">Protein Structure</Keyword><Keyword MajorTopicYN="N">SARS</Keyword><Keyword MajorTopicYN="N">Structural Biology</Keyword><Keyword MajorTopicYN="N">Viral Protein</Keyword><Keyword MajorTopicYN="N">Virus Assembly</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>3</Month><Day>27</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>3</Month><Day>29</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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