ArticleProtein science : a publication of the Protein Society2010
Use of protein trans-splicing to produce active and segmentally (2)H, (15)N labeled mannuronan C5-epimerase AlgE4.
Article in Protein science : a publication of the Protein Society, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed, 14 citations in OpenAlex.
- Identification of a Pivotal Residue for Determining the Block Structure-Forming Properties of Alginate C-5 Epimerases.ACS omega · 2020Article
- NMR Structure and Dynamics of TonB Investigated by Scar-Less Segmental Isotopic Labeling Using a Salt-Inducible Split Intein.Frontiers in chemistry · 2020Article
- Characterizing Aciniform Silk Repetitive Domain Backbone Dynamics and Hydrodynamic Modularity.International journal of molecular sciences · 2016Article
- Structural and functional characterization of the R-modules in alginate C-5 epimerases AlgE4 and AlgE6 from Azotobacter vinelandii.The Journal of biological chemistry · 2014Article
- Structure-based engineering and comparison of novel split inteins for protein ligation.Molecular bioSystems · 2014Article
- SPLICEFINDER - a fast and easy screening method for active protein trans-splicing positions.PloS one · 2013Article
- Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing.Journal of biomolecular NMR · 2012Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
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No grant is acknowledged in the PubMed record.
Abstract
Alginate epimerases are large multidomain proteins capable of epimerising C5 on beta-D-mannuronic acid (M) turning it into alpha-L-guluronic acid (G) in a polymeric alginate. Azotobacter vinelandii secretes a family of seven epimerases, each of which is capable of producing alginates with characteristic G distribution patterns. All seven epimerases consist of two types of modules, denoted A and R, in varying numbers. Attempts to study these enzymes with solution-state NMR are hampered by their size-the smallest epimerase, AlgE4, consisting of one A- and one R-module, is 58 kDa, resulting in heavy signal overlap impairing the interpretation of NMR spectra. Thus we obtained segmentally (2)H, (15)N labeled AlgE4 isotopomeres (A-[(2)H, (15)N]-R and [(2)H, (15)N]-A-R) by protein trans-splicing using the naturally split intein of Nostoc punctiforme. The NMR spectra of native AlgE4 and the ligated versions coincide well proving the conservation of protein structure. The activity of the ligated AlgE4 was verified by two different enzyme activity assays, demonstrating that ligated AlgE4 displays the same catalytic activity as wild-type AlgE4.
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