ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of the secretion domain of HxuA from Haemophilus influenzae.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
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- Repeat modules and N-linked glycans define structure and antigenicity of a critical enterotoxigenicbioRxiv : the preprint server for biology · 2024Article
- Marine prebiotics mediate decolonization of Pseudomonas aeruginosa from gut by inhibiting secreted virulence factor interactions with mucins and enriching Bacteroides population.Journal of biomedical science · 2023Article
- A novel class of Candida glabrata cell wall proteins with β-helix fold mediates adhesion in clinical isolates.PLoS pathogens · 2021Article
- Semiprocessive Hyperglycosylation of Adhesin by Bacterial ProteinACS chemical biology · 2021Article
- Characterization of Awp14, A Novel Cluster III Adhesin Identified in a High Biofilm-FormingFrontiers in cellular and infection microbiology · 2021Article
- Review
- Modeling oblong proteins and water-mediated interfaces with RosettaDock in CAPRI rounds 28-35.Proteins · 2017Article
- Proteolysis of truncated hemolysin A yields a stable dimerization interface.Acta crystallographica. Section F, Structural biology communications · 2017Article
- Article
- Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions.Frontiers in cellular and infection microbiology · 2017Review
- Heme Synthesis and Acquisition in Bacterial Pathogens.Journal of molecular biology · 2016Review
- Structural basis for haem piracy from host haemopexin by Haemophilus influenzae.Nature communications · 2016Article
- Structural determinants of the interaction between the TpsA and TpsB proteins in the Haemophilus influenzae HMW1 two-partner secretion system.Journal of bacteriology · 2015Article
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4 authors.
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Abstract
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.
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