Structure of the secretion domain of HxuA ...
Document type :
Article dans une revue scientifique
PMID :
Permalink :
Title :
Structure of the secretion domain of HxuA from Haemophilus influenzae
Author(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]

Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Villeret, Vincent [Auteur]

Institut de Recherche Interdisciplinaire [Villeneuve d'Ascq] [IRI]
Journal title :
Acta Crystallographica. Section F, Structural Biology and Crystallization Communications
Abbreviated title :
Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun.
Volume number :
69
Pages :
1322-1327
Publication date :
2013-12
ISSN :
1744-3091
English keyword(s) :
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
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Audience :
Non spécifiée
Administrative institution(s) :
CNRS
Université de Lille
Université de Lille
Collections :
Research team(s) :
Biologie structurale et intégrative
Submission date :
2020-02-12T15:11:31Z
2021-03-26T08:55:32Z
2021-03-26T08:55:32Z