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Hemsworth G.R.,University of York | Henrissat B.,CNRS Architecture and Functions of Biological Macromolecules Lab | Davies G.J.,University of York | Walton P.H.,University of York
Nature chemical biology | Year: 2014

Lytic polysaccharide monooxygenases (LPMOs) are a recently discovered class of enzymes capable of oxidizing recalcitrant polysaccharides. They are attracting considerable attention owing to their potential use in biomass conversion, notably in the production of biofuels. Previous studies have identified two discrete sequence-based families of these enzymes termed AA9 (formerly GH61) and AA10 (formerly CBM33). Here, we report the discovery of a third family of LPMOs. Using a chitin-degrading exemplar from Aspergillus oryzae, we show that the three-dimensional structure of the enzyme shares some features of the previous two classes of LPMOs, including a copper active center featuring the 'histidine brace' active site, but is distinct in terms of its active site details and its EPR spectroscopy. The newly characterized AA11 family expands the LPMO clan, potentially broadening both the range of potential substrates and the types of reactive copper-oxygen species formed at the active site of LPMOs.

Longhi S.,CNRS Architecture and Functions of Biological Macromolecules Lab
Advances in Experimental Medicine and Biology | Year: 2012

In this chapter, I focus on the biochemical and structural characterization of the complex between the intrinsically disordered C-terminal domain of the measles virus nucleoprotein (N TAIL) and the C-terminal X domain (XD) of the viral phosphoprotein (P). I summarize the main experimental data available so far pointing out the prevalently disordered nature of N TAIL even after complex formation and the role of the flexible C-terminal appendage in the binding reaction. I finally discuss the possible functional role of these residual disordered regions within the complex in terms of their ability to capture other regulatory, binding partners. © 2012 Landes Bioscience and Springer Science+Business Media.

Vincentelli R.,CNRS Architecture and Functions of Biological Macromolecules Lab | Romier C.,University of Strasbourg
Current Opinion in Structural Biology | Year: 2013

Escherichia coli is the major expression host for the production of homogeneous protein samples for structural studies. The introduction of high-throughput technologies in the last decade has further revitalized E. coli expression, with rapid assessment of different expression strategies and successful production of an ever-increasing number of proteins. In addition, miniaturization of biophysical characterizations should soon help choosing expression strategies based on quantitative and qualitative observations. Since many proteins form larger assemblies in vivo, dedicated co-expression systems for E. coli are now addressing the reconstitution of protein complexes. Yet, co-expression approaches show an increasing experimental combinatorial intricacy when considering larger complexes. The current combination of high-throughput and co-expression technologies paves the way, however, for tackling larger and more complex macromolecular assemblies. © 2013.

Medie F.M.,Aix - Marseille University | Medie F.M.,CNRS Architecture and Functions of Biological Macromolecules Lab | Davies G.J.,University of York | Drancourt M.,Aix - Marseille University | Henrissat B.,CNRS Architecture and Functions of Biological Macromolecules Lab
Nature Reviews Microbiology | Year: 2012

Cellulolytic enzymes have been the subject of renewed interest owing to their potential role in the conversion of plant lignocellulose to sustainable biofuels. An analysis of ∼1,500 complete bacterial genomes, presented here, reveals that ∼40% of the genomes of sequenced bacteria encode at least one cellulase gene. Most of the bacteria that encode cellulases are soil and marine saprophytes, many of which encode a range of enzymes for cellulose hydrolysis and also for the breakdown of the other constituents of plant cell walls (hemicelluloses and pectins). Intriguingly, cellulases are present in organisms that are usually considered as non-saprophytic, such as Mycobacterium tuberculosis, Legionella pneumophila, Yersinia pestis and even Escherichia coli. We also discuss newly emerging roles of cellulases in such non-saprophytic organisms. © 2012 Macmillan Publishers Limited. All rights reserved.

Habchi J.,Aix - Marseille University | Habchi J.,CNRS Architecture and Functions of Biological Macromolecules Lab | Tompa P.,Vrije Universiteit Brussel | Tompa P.,Hungarian Academy of Sciences | And 4 more authors.
Chemical Reviews | Year: 2014

Proteins are the major component of the living cell. They play crucial roles in the maintenance of life, and their dysfunctions are known to cause different pathologies. Simple amino acid propensities reflect some basic physical or sequence features. Such propensity-based predictors rely on simple statistics of amino acid propensity, on the physical/chemical features of amino acids, or on a preliminary concept on the physical background of disorder. Regions of missing electron density in the PDB are generally short, as long regions prevent crystallization. As such, short disorder is overrepresented in the database of disordered regions, and hence these predictors tend to perform better in predicting short disorder than long disorder. Predictors can also be classified based on the binary nature of the prediction. Examples of binary predictors are the CH plot and the cumulative distribution function (CDF) analysis.

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