Structural basis of protein asn-glycosylation by oligosaccharyltransferases

    Research output: Chapter in Book/Report/Conference proceedingChapter

    1 Citation (Scopus)

    Abstract

    Glycosylation of asparagine residues is a ubiquitous protein modification. This N-glycosylation is essential in Eukaryotes, but principally nonessential in Prokaryotes (Archaea and Eubacteria), although it facilitates their survival and pathogenicity. In many reviews, Archaea have received far less attention than Eubacteria, but this review will cover the N-glycosylation in the three domains of life. The oligosaccharide chain is preassembled on a lipid-phospho carrier to form a donor substrate, lipid-linked oligosaccharide (LLO). The en bloc transfer of an oligosaccharide from LLO to selected Asn residues in the Asn-X-Ser/Thr (X≠Pro) sequons in a polypeptide chain is catalyzed by a membrane-bound enzyme, oligosaccharyltransferase (OST). Over the last 10 years, the three-dimensional structures of the catalytic subunits of the Stt3/AglB/PglB proteins, with an acceptor peptide and a donor LLO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions of OSTs. A catalytic structure in the TM region accounts for the amide bond twisting, which increases the reactivity of the side-chain nitrogen atom of the acceptor Asn residue in the sequon. The Ser/Thr-binding pocket in the C-terminal domain explains the requirement for hydroxy amino acid residues in the sequon. As expected, the two functional structures are formed by the involvement of short amino acid motifs conserved across the three domains of life.

    Original languageEnglish
    Title of host publicationAdvances in Experimental Medicine and Biology
    PublisherSpringer New York LLC
    Pages171-199
    Number of pages29
    DOIs
    Publication statusPublished - Jan 1 2018

    Publication series

    NameAdvances in Experimental Medicine and Biology
    Volume1104
    ISSN (Print)0065-2598
    ISSN (Electronic)2214-8019

    Fingerprint

    Glycosylation
    Archaea
    Oligosaccharides
    Bacteria
    Cryoelectron Microscopy
    Amino Acids
    Peptides
    Amino Acid Motifs
    Hydroxy Acids
    Proteins
    Asparagine
    X ray crystallography
    X Ray Crystallography
    Eukaryota
    Amides
    Electron microscopy
    Virulence
    Catalytic Domain
    Nitrogen
    Membranes

    All Science Journal Classification (ASJC) codes

    • Biochemistry, Genetics and Molecular Biology(all)

    Cite this

    Kohda, D. (2018). Structural basis of protein asn-glycosylation by oligosaccharyltransferases. In Advances in Experimental Medicine and Biology (pp. 171-199). (Advances in Experimental Medicine and Biology; Vol. 1104). Springer New York LLC. https://doi.org/10.1007/978-981-13-2158-0_9

    Structural basis of protein asn-glycosylation by oligosaccharyltransferases. / Kohda, Daisuke.

    Advances in Experimental Medicine and Biology. Springer New York LLC, 2018. p. 171-199 (Advances in Experimental Medicine and Biology; Vol. 1104).

    Research output: Chapter in Book/Report/Conference proceedingChapter

    Kohda, D 2018, Structural basis of protein asn-glycosylation by oligosaccharyltransferases. in Advances in Experimental Medicine and Biology. Advances in Experimental Medicine and Biology, vol. 1104, Springer New York LLC, pp. 171-199. https://doi.org/10.1007/978-981-13-2158-0_9
    Kohda D. Structural basis of protein asn-glycosylation by oligosaccharyltransferases. In Advances in Experimental Medicine and Biology. Springer New York LLC. 2018. p. 171-199. (Advances in Experimental Medicine and Biology). https://doi.org/10.1007/978-981-13-2158-0_9
    Kohda, Daisuke. / Structural basis of protein asn-glycosylation by oligosaccharyltransferases. Advances in Experimental Medicine and Biology. Springer New York LLC, 2018. pp. 171-199 (Advances in Experimental Medicine and Biology).
    @inbook{94ef659daab34a39bfd7eed2cc0e7a18,
    title = "Structural basis of protein asn-glycosylation by oligosaccharyltransferases",
    abstract = "Glycosylation of asparagine residues is a ubiquitous protein modification. This N-glycosylation is essential in Eukaryotes, but principally nonessential in Prokaryotes (Archaea and Eubacteria), although it facilitates their survival and pathogenicity. In many reviews, Archaea have received far less attention than Eubacteria, but this review will cover the N-glycosylation in the three domains of life. The oligosaccharide chain is preassembled on a lipid-phospho carrier to form a donor substrate, lipid-linked oligosaccharide (LLO). The en bloc transfer of an oligosaccharide from LLO to selected Asn residues in the Asn-X-Ser/Thr (X≠Pro) sequons in a polypeptide chain is catalyzed by a membrane-bound enzyme, oligosaccharyltransferase (OST). Over the last 10 years, the three-dimensional structures of the catalytic subunits of the Stt3/AglB/PglB proteins, with an acceptor peptide and a donor LLO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions of OSTs. A catalytic structure in the TM region accounts for the amide bond twisting, which increases the reactivity of the side-chain nitrogen atom of the acceptor Asn residue in the sequon. The Ser/Thr-binding pocket in the C-terminal domain explains the requirement for hydroxy amino acid residues in the sequon. As expected, the two functional structures are formed by the involvement of short amino acid motifs conserved across the three domains of life.",
    author = "Daisuke Kohda",
    year = "2018",
    month = "1",
    day = "1",
    doi = "10.1007/978-981-13-2158-0_9",
    language = "English",
    series = "Advances in Experimental Medicine and Biology",
    publisher = "Springer New York LLC",
    pages = "171--199",
    booktitle = "Advances in Experimental Medicine and Biology",

    }

    TY - CHAP

    T1 - Structural basis of protein asn-glycosylation by oligosaccharyltransferases

    AU - Kohda, Daisuke

    PY - 2018/1/1

    Y1 - 2018/1/1

    N2 - Glycosylation of asparagine residues is a ubiquitous protein modification. This N-glycosylation is essential in Eukaryotes, but principally nonessential in Prokaryotes (Archaea and Eubacteria), although it facilitates their survival and pathogenicity. In many reviews, Archaea have received far less attention than Eubacteria, but this review will cover the N-glycosylation in the three domains of life. The oligosaccharide chain is preassembled on a lipid-phospho carrier to form a donor substrate, lipid-linked oligosaccharide (LLO). The en bloc transfer of an oligosaccharide from LLO to selected Asn residues in the Asn-X-Ser/Thr (X≠Pro) sequons in a polypeptide chain is catalyzed by a membrane-bound enzyme, oligosaccharyltransferase (OST). Over the last 10 years, the three-dimensional structures of the catalytic subunits of the Stt3/AglB/PglB proteins, with an acceptor peptide and a donor LLO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions of OSTs. A catalytic structure in the TM region accounts for the amide bond twisting, which increases the reactivity of the side-chain nitrogen atom of the acceptor Asn residue in the sequon. The Ser/Thr-binding pocket in the C-terminal domain explains the requirement for hydroxy amino acid residues in the sequon. As expected, the two functional structures are formed by the involvement of short amino acid motifs conserved across the three domains of life.

    AB - Glycosylation of asparagine residues is a ubiquitous protein modification. This N-glycosylation is essential in Eukaryotes, but principally nonessential in Prokaryotes (Archaea and Eubacteria), although it facilitates their survival and pathogenicity. In many reviews, Archaea have received far less attention than Eubacteria, but this review will cover the N-glycosylation in the three domains of life. The oligosaccharide chain is preassembled on a lipid-phospho carrier to form a donor substrate, lipid-linked oligosaccharide (LLO). The en bloc transfer of an oligosaccharide from LLO to selected Asn residues in the Asn-X-Ser/Thr (X≠Pro) sequons in a polypeptide chain is catalyzed by a membrane-bound enzyme, oligosaccharyltransferase (OST). Over the last 10 years, the three-dimensional structures of the catalytic subunits of the Stt3/AglB/PglB proteins, with an acceptor peptide and a donor LLO, have been determined by X-ray crystallography, and recently the complex structures with other subunits have been determined by cryo-electron microscopy. Structural comparisons within the same species and across the different domains of life yielded a unified view of the structures and functions of OSTs. A catalytic structure in the TM region accounts for the amide bond twisting, which increases the reactivity of the side-chain nitrogen atom of the acceptor Asn residue in the sequon. The Ser/Thr-binding pocket in the C-terminal domain explains the requirement for hydroxy amino acid residues in the sequon. As expected, the two functional structures are formed by the involvement of short amino acid motifs conserved across the three domains of life.

    UR - http://www.scopus.com/inward/record.url?scp=85057228461&partnerID=8YFLogxK

    UR - http://www.scopus.com/inward/citedby.url?scp=85057228461&partnerID=8YFLogxK

    U2 - 10.1007/978-981-13-2158-0_9

    DO - 10.1007/978-981-13-2158-0_9

    M3 - Chapter

    C2 - 30484249

    AN - SCOPUS:85057228461

    T3 - Advances in Experimental Medicine and Biology

    SP - 171

    EP - 199

    BT - Advances in Experimental Medicine and Biology

    PB - Springer New York LLC

    ER -