The complete enzymatic hydrolysis of mannan polysaccharides requires at least three types of enzymes working synergistically: ²-mannanase, ²-mannosidase, and ²-glucosidase. The hyperthermophilic bacterium Thermotoga petrophila produces the enzyme endo-²-1,4-mannanse (TpMan), which is composed of a GH5 catalytic domain and a carbohydrate-binding domain connected through a linker. The crystal structure of the GH5 catalytic domain was determined, however, to date, there is no three-dimensional structure available for the full-length TpMan. Recently, we reported the first low-resolution model for the full-length TpMan and demonstrated that the linker is a compact domain. In this scientific project, as part of a continuing investigation of TpMan, we propose to determine the three-dimensional structure of the full-length enzyme (TpMan) and/or of its central domain (linker) using X-ray crystallography. Our previous attempts to crystallize the full-length TpMan and the linker were so far unsuccessful. Therefore, an internship in a center such as the Institut de Biologie Structurale - Grenoble/France with extensive experience in X-ray crystallography, should certainly be essential in determining the TpMan structure.
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