ArticleThe Journal of biological chemistry2016
The Klebsiella pneumoniae O12 ATP-binding Cassette (ABC) Transporter Recognizes the Terminal Residue of Its O-antigen Polysaccharide Substrate.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 30 citations in OpenAlex.
- Klebsiella pneumoniae O-polysaccharide biosynthesis highlights the diverse organization of catalytic modules in ABC transporter-dependent glycan assembly.The Journal of biological chemistry · 2024Article
- Identification of a second glycoform of the clinically prevalent O1 antigen fromProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular basis for polysaccharide recognition and modulated ATP hydrolysis by the O antigen ABC transporter.Nature communications · 2022Article
- A Molecular Perspective on Colistin andDiagnostics (Basel, Switzerland) · 2021Review
- An ABC transporter Wzm-Wzt catalyzes translocation of lipid-linked galactan across the plasma membrane in mycobacteria.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Cryo-EM structure of the full-length WzmWzt ABC transporter required for lipid-linked O antigen transport.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure and genetics of Escherichia coli O antigens.FEMS microbiology reviews · 2020Review
- Lipopolysaccharide O-antigens-bacterial glycans made to measure.The Journal of biological chemistry · 2020Review
- Cryo-electron Microscopy Structure and Transport Mechanism of a Wall Teichoic Acid ABC Transporter.mBio · 2020Article
- Analysis of the Topology and Active-Site Residues of WbbF, a Putative O-Polysaccharide Synthase from Salmonella enterica Serovar Borreze.Journal of bacteriology · 2020Article
- Structure and Ligand-Binding Properties of the O Antigen ABC Transporter Carbohydrate-Binding Domain.Structure (London, England : 1993) · 2020Article
- Substrate recognition by a carbohydrate-binding module in the prototypical ABC transporter for lipopolysaccharide O-antigen fromThe Journal of biological chemistry · 2019Article
- Article
- A lipid gating mechanism for the channel-forming O antigen ABC transporter.Nature communications · 2019Article
- Article
- Crystal structure of the DNA-binding domain of Myelin-gene Regulatory Factor.Scientific reports · 2017Article
- Single polysaccharide assembly protein that integrates polymerization, termination, and chain-length quality control.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Dectin-2 Recognizes Mannosylated O-antigens of Human Opportunistic Pathogens and Augments Lipopolysaccharide Activation of Myeloid Cells.The Journal of biological chemistry · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Export of the Escherichia coli serotype O9a O-antigenic polysaccharides (O-PS) involves an ATP-binding cassette (ABC) transporter. The process requires a non-reducing terminal residue, which is recognized by a carbohydrate-binding module (CBM) appended to the C terminus of the nucleotide-binding domain of the transporter. Here, we investigate the process in Klebsiella pneumoniae serotype O12 (and Raoultella terrigena ATCC 33257). The O12 polysaccharide is terminated at the non-reducing end by a β-linked 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) residue. The O12 ABC transporter also binds its cognate O-PS via a CBM, and export is dependent on the presence of the terminal β-Kdo residue. The overall structural architecture of the O12 CBM resembles the O9a prototype, but they share only weak sequence similarity, and the putative binding pocket for the O12 glycan is different. Removal of the CBM abrogated O-PS transport, but export was restored when the CBM was expressed in trans with the mutant CBM-deficient ABC transporter. These results demonstrate that the CBM-mediated substrate-recognition mechanism is evolutionarily conserved and can operate with glycans of widely differing structures.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.