Structure of the secretion domain of HxuA ...
Type de document :
Article dans une revue scientifique
PMID :
URL permanente :
Titre :
Structure of the secretion domain of HxuA from Haemophilus influenzae
Auteur(s) :
Baelen, Stéphanie [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Dewitte, Frederique [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Clantin, Bernard [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Villeret, Vincent [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Dewitte, Frederique [Auteur]
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Clantin, Bernard [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Villeret, Vincent [Auteur]
![refId](/themes/Mirage2//images/idref.png)
Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Titre de la revue :
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Nom court de la revue :
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Numéro :
69
Pagination :
1322-1327
Date de publication :
2013-12
ISSN :
1744-3091
Mot(s)-clé(s) en anglais :
Amino Acid Sequence
Gene Expression
Bacterial Outer Membrane Proteins
Protein Structure, Secondary
Bacterial Secretion Systems
X-ray Crystallography
Escherichia coli
Models, Molecular
Molecular Sequence Data
Hemopexin
secretion system
Recombinant Proteins
Haemophilus influenzae
Sequence Alignment
TPS
Heme
Protein Binding
β-helix
Protein Interaction Domains and Motifs
Structural Homology, Protein
HxuA
Carrier Proteins
Gene Expression
Bacterial Outer Membrane Proteins
Protein Structure, Secondary
Bacterial Secretion Systems
X-ray Crystallography
Escherichia coli
Models, Molecular
Molecular Sequence Data
Hemopexin
secretion system
Recombinant Proteins
Haemophilus influenzae
Sequence Alignment
TPS
Heme
Protein Binding
β-helix
Protein Interaction Domains and Motifs
Structural Homology, Protein
HxuA
Carrier Proteins
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
Haemophilus influenzae HxuA is a cell-surface protein with haem-haemopexin binding activity which is key to haem acquisition from haemopexin and thus is one of the potential sources of haem for this microorganism. HxuA is ...
Lire la suite >Haemophilus influenzae HxuA is a cell-surface protein with haem-haemopexin binding activity which is key to haem acquisition from haemopexin and thus is one of the potential sources of haem for this microorganism. HxuA is secreted by its specific transporter HxuB. HxuA/HxuB belongs to the so-called two-partner secretion systems (TPSs) that are characterized by a conserved N-terminal domain in the secreted protein which is essential for secretion. Here, the 1.5 Å resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a β-helix domain with two extra-helical motifs, a four-stranded β-sheet and an N-terminal cap. Comparisons with other structures of TpsA secretion domains are reported. They reveal that despite limited sequence identity, strong structural similarities are found between the β-helix motifs, consistent with the idea that the TPS domain plays a role not only in the interaction with the specific TpsB partners but also as the scaffold initiating progressive folding of the TpsA proteins at the bacterial surface.Lire moins >
Lire la suite >Haemophilus influenzae HxuA is a cell-surface protein with haem-haemopexin binding activity which is key to haem acquisition from haemopexin and thus is one of the potential sources of haem for this microorganism. HxuA is secreted by its specific transporter HxuB. HxuA/HxuB belongs to the so-called two-partner secretion systems (TPSs) that are characterized by a conserved N-terminal domain in the secreted protein which is essential for secretion. Here, the 1.5 Å resolution structure of the secretion domain of HxuA, HxuA301, is reported. The structure reveals that HxuA301 folds into a β-helix domain with two extra-helical motifs, a four-stranded β-sheet and an N-terminal cap. Comparisons with other structures of TpsA secretion domains are reported. They reveal that despite limited sequence identity, strong structural similarities are found between the β-helix motifs, consistent with the idea that the TPS domain plays a role not only in the interaction with the specific TpsB partners but also as the scaffold initiating progressive folding of the TpsA proteins at the bacterial surface.Lire moins >
Langue :
Anglais
Audience :
Non spécifiée
Établissement(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Équipe(s) de recherche :
Biologie structurale et intégrative
Date de dépôt :
2020-02-12T15:11:31Z
2021-03-26T08:55:32Z
2021-03-26T08:55:32Z