Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution
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Crystal structure of the C-terminal globular domain of the third paralog of the Archaeoglobus fulgidus oligosaccharyltransferasesCrystal structures of an archaeal oligosaccharyltransferase provide insights into the catalytic cycle of N-linked protein glycosylationStructural basis for catalysis at the membrane-water interface.N-linked glycosylation in Archaea: a structural, functional, and genetic analysis.Hot and sweet: protein glycosylation in Crenarchaeota.Structural insights from random mutagenesis of Campylobacter jejuni oligosaccharyltransferase PglB.N-Linked Glycans Are Assembled on Highly Reduced Dolichol Phosphate Carriers in the Hyperthermophilic Archaea Pyrococcus furiosus.Complementation of an aglB Mutant of Methanococcus maripaludis with Heterologous Oligosaccharyltransferases.Biochemical evidence for an alternate pathway in N-linked glycoprotein biosynthesisComparative Analysis of Archaeal Lipid-linked Oligosaccharides That Serve as Oligosaccharide Donors for Asn Glycosylation.Emerging facets of prokaryotic glycosylation.Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.Add salt, add sugar: N-glycosylation in Haloferax volcanii.Advances in understanding glycosyltransferases from a structural perspective.In silico Investigation of the PglB Active Site Reveals Transient Catalytic States and Octahedral Metal Ion Coordination.Glycosyltransferases: mechanisms and applications in natural product development.Lipid sugar carriers at the extremes: The phosphodolichols Archaea use in N-glycosylation.Rational design of crystal contact-free space in protein crystals for analyzing spatial distribution of motions within protein molecules.ArnT proteins that catalyze the glycosylation of lipopolysaccharide share common features with bacterial N-oligosaccharyltransferases.Two distinct N-glycosylation pathways process the Haloferax volcanii S-layer glycoprotein upon changes in environmental salinitySubstrate promiscuity: AglB, the archaeal oligosaccharyltransferase, can process a variety of lipid-linked glycans.AglB, catalyzing the oligosaccharyl transferase step of the archaeal N-glycosylation process, is essential in the thermoacidophilic crenarchaeon Sulfolobus acidocaldarius.
P2860
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P2860
Crystal structure of the C-terminal globular domain of oligosaccharyltransferase from Archaeoglobus fulgidus at 1.75 Å resolution
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2012 nî lūn-bûn
@nan
2012 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2012 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
name
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@ast
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@en
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@nl
type
label
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@ast
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@en
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@nl
prefLabel
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@ast
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@en
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@nl
P2093
P356
P1433
P1476
Crystal structure of the C-ter ...... fulgidus at 1.75 Å resolution
@en
P2093
Daisuke Kohda
James Nyirenda
Masaki Matsumoto
Mayumi Igura
Nobuo Noda
Satoru Yuzawa
Shunsuke Matsumoto
P304
P356
10.1021/BI300076U
P407
P577
2012-05-22T00:00:00Z