ArticleStructure (London, England : 1993)2008
Solution structure of Alg13: the sugar donor subunit of a yeast N-acetylglucosamine transferase.
Article in Structure (London, England : 1993), 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 39 citations in OpenAlex.
- N-Glycosylation-The Behind-the-Scenes 'Manipulative Hand' of Plant Pathogen Invasiveness.Molecular plant pathology · 2025Review
- ALG13-Congenital Disorder of Glycosylation (ALG13-CDG): Updated clinical and molecular review and clinical management guidelines.Molecular genetics and metabolism · 2024Review
- The Search for Cryptic L-Rhamnosyltransferases on theJournal of fungi (Basel, Switzerland) · 2022Article
- Agl24 is an ancient archaeal homolog of the eukaryotic N-glycan chitobiose synthesis enzymes.eLife · 2022Article
- Structural Analysis of the Effect of Asn107Ser Mutation on Alg13 Activity and Alg13-Alg14 Complex Formation and Expanding the Phenotypic Variability of ALG13-CDG.Biomolecules · 2022Article
- Predominant and novel de novo variants in 29 individuals with ALG13 deficiency: Clinical description, biomarker status, biochemical analysis, and treatment suggestions.Journal of inherited metabolic disease · 2020Article
- Distinct expression and prognostic value of OTU domain-containing proteins in non-small-cell lung cancer.Oncology letters · 2019Article
- Perspectives on Glycosylation and Its Congenital Disorders.Trends in genetics : TIG · 2018Review
- Structure-function relationships of membrane-associated GT-B glycosyltransferases.Glycobiology · 2014Review
- An engineered eukaryotic protein glycosylation pathway in Escherichia coli.Nature chemical biology · 2012Article
- The expanding horizons of asparagine-linked glycosylation.Biochemistry · 2011Review
- Molecular basis of phosphatidyl-myo-inositol mannoside biosynthesis and regulation in mycobacteria.The Journal of biological chemistry · 2010Review
- NMR structure determination for larger proteins using backbone-only data.Science (New York, N.Y.) · 2010Article
- Substrate-induced conformational changes in the essential peripheral membrane-associated mannosyltransferase PimA from mycobacteria: implications for catalysis.The Journal of biological chemistry · 2009Article
- Hetero-oligomeric interactions between early glycosyltransferases of the dolichol cycle.Glycobiology · 2009Article
- Chapter 2: Biogenesis of the cell wall and other glycoconjugates of Mycobacterium tuberculosis.Advances in applied microbiology · 2009Review
- Interaction between the C termini of Alg13 and Alg14 mediates formation of the active UDP-N-acetylglucosamine transferase complex.The Journal of biological chemistry · 2008Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
Abstract
The solution structure of Alg13, the glycosyl donor-binding domain of an important bipartite glycosyltransferase in the yeast Saccharomyces cerevisiae, is presented. This glycosyltransferase is unusual in that it is active only in the presence of a binding partner, Alg14. Alg13 is found to adopt a unique topology among glycosyltransferases. Rather than the conventional Rossmann fold found in all GT-B enzymes, the N-terminal half of the protein is a Rossmann-like fold with a mixed parallel and antiparallel beta sheet. The Rossmann fold of the C-terminal half of Alg13 is conserved. However, although conventional GT-B enzymes usually possess three helices at the C terminus, only two helices are present in Alg13. Titration of Alg13 with both UDP-GlcNAc, the native glycosyl donor, and a paramagnetic mimic, UDP-TEMPO, shows that the interaction of Alg13 with the sugar donor is primarily through the residues in the C-terminal half of the protein.
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Registered trials
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.