Literature DB >> 28417374

Probing the Complex Architecture of Multimodular Carbohydrate-Active Enzymes Using a Combination of Small Angle X-Ray Scattering and X-Ray Crystallography.

Mirjam Czjzek1, Elizabeth Ficko-Blean2.   

Abstract

The various modules in multimodular carbohydrate-active enzymes (CAZymes) may function in catalysis, carbohydrate binding, protein-protein interactions or as linkers. Here, we describe how combining the biophysical techniques of Small Angle X-ray Scattering (SAXS) and macromolecular X-ray crystallography (XRC) provides a powerful tool for examination into questions related to overall structural organization of ultra multimodular CAZymes.

Entities:  

Keywords:  CAZymes; CBM; Carbohydrate binding module; Carbohydrate-active enzymes; Cohesin; Dissect and build; Dockerin; Glycoside hydrolase; Multimodular; SAXS; Small-angle X-ray scattering; Structure; X-ray Crystallography

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Year:  2017        PMID: 28417374     DOI: 10.1007/978-1-4939-6899-2_19

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  2 in total

1.  The carbohydrate-binding module and linker of a modular lytic polysaccharide monooxygenase promote localized cellulose oxidation.

Authors:  Gaston Courtade; Zarah Forsberg; Ellinor B Heggset; Vincent G H Eijsink; Finn L Aachmann
Journal:  J Biol Chem       Date:  2018-07-02       Impact factor: 5.157

Review 2.  Carbohydrate active enzyme domains from extreme thermophiles: components of a modular toolbox for lignocellulose degradation.

Authors:  Jonathan Botha; Eshchar Mizrachi; Alexander A Myburg; Don A Cowan
Journal:  Extremophiles       Date:  2017-11-06       Impact factor: 2.395

  2 in total

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