Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases - Wikidata - awgldk - TriplyDB

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

http://www.wikidata.org/entity/Q27646588

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Computational enzyme design approaches with significant biological outcomes: progress and challenges Structure of human POFUT2: insights into thrombospondin type 1 repeat fold and O-fucosylation Substrate and Metal Ion Promiscuity in Mannosylglycerate Synthase X-ray structure of a bacterial oligosaccharyltransferase Eukaryotic N-Glycosylation Occurs via the Membrane-anchored C-terminal Domain of the Stt3p Subunit of Oligosaccharyltransferase Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferases Crystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylation Glycosyltransferase structural biology and its role in the design of catalysts for glycosylation Analyzing protein structure and function using ancestral gene reconstruction Structural basis for catalysis at the membrane-water interface.N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Computational analysis reveals abundance of potential glycoproteins in Archaea, Bacteria and Eukarya.The s-layer glycome-adding to the sugar coat of bacteria.Characterization of the structurally diverse N-linked glycans of Campylobacter species.Hot and sweet: protein glycosylation in Crenarchaeota.GlycoPP: a webserver for prediction of N- and O-glycosites in prokaryotic protein sequences.Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB.The expanding horizons of asparagine-linked glycosylation.Exploiting topological constraints to reveal buried sequence motifs in the membrane-bound N-linked oligosaccharyl transferases.An inside-out origin for the eukaryotic cell.Identification of genes involved in the acetamidino group modification of the flagellin N-linked glycan of Methanococcus maripaludis.Complementation of an aglB Mutant of Methanococcus maripaludis with Heterologous Oligosaccharyltransferases.Mechanism of bacterial oligosaccharyltransferase: in vitro quantification of sequon binding and catalysis Comparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation.The multiple evolutionary origins of the eukaryotic N-glycosylation pathway.Protein glycosylation in Archaea: sweet and extreme.Analogies and homologies in lipopolysaccharide and glycoprotein biosynthesis in bacteria.Bacterial protein N-glycosylation: new perspectives and applications.In silico Investigation of the PglB Active Site Reveals Transient Catalytic States and Octahedral Metal Ion Coordination.Agl16, a thermophilic glycosyltransferase mediating the last step of N-Glycan biosynthesis in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius ArnT proteins that catalyze the glycosylation of lipopolysaccharide share common features with bacterial N-oligosaccharyltransferases.Optimized protocol for expression and purification of membrane-bound PglB, a bacterial oligosaccharyl transferase.Selective control of oligosaccharide transfer efficiency for the N-glycosylation sequon by a point mutation in oligosaccharyltransferase.Diversity in prokaryotic glycosylation: an archaeal-derived N-linked glycan contains legionaminic acid.Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinity Substrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.Biosynthesis and role of N-linked glycosylation in cell surface structures of archaea with a focus on flagella and s layers.A novel and simple method of production and biophysical characterization of a mini-membrane protein, Ost4p: a subunit of yeast oligosaccharyl transferase AglB, catalyzing the oligosaccharyl transferase step of the archaeal N-glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.Asn-linked oligosaccharide chain of a crenarchaeon, Pyrobaculum calidifontis, is reminiscent of the eukaryotic high-mannose-type glycan.

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Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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description

2010 nî lūn-bûn

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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած

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2010 թվականի փետրվարին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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name

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

@en

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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type

label

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

@en

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

@nl

prefLabel

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

@en

Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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JBC.M109.081752

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Journal of Biological Chemistry

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Comparative Structural Biology of Eubacterial and Archaeal Oligosaccharyltransferases

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Daisuke Kohda

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James Nyirenda

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Jun Kamishikiryo

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Mayumi Igura

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Nobuo Maita

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P2860

Ribophorin I acts as a substrate-specific facilitator of N-glycosylation

Cotranslational and posttranslational N-glycosylation of polypeptides by distinct mammalian OST isoforms

MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform

Ribophorin I regulates substrate delivery to the oligosaccharyltransferase core

GASH: an improved algorithm for maximizing the number of equivalent residues between two protein structures.

Crystallography & NMR System: A New Software Suite for Macromolecular Structure Determination

Processing of X-ray diffraction data collected in oscillation mode

Oxidoreductase activity of oligosaccharyltransferase subunits Ost3p and Ost6p defines site-specific glycosylation efficiency

Structure-guided identification of a new catalytic motif of oligosaccharyltransferase

Coot: model-building tools for molecular graphics

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4941-50

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10.1074/JBC.M109.081752

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285

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20007322

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2836098

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