%0 Figure %A Morrill, Johan %A Kulcinskaja, Evelina %A Sulewska, Anna %A Lahtinen, Sampo %A Stülbrand, Henrik %A Svensson, Birte %A Hachem, Maher Abou %D 2015 %T Additional file 13: of The GH5 1,4-β-mannanase from Bifidobacterium animalis subsp. lactis Bl-04 possesses a low-affinity mannan-binding module and highlights the diversity of mannanolytic enzymes %U https://springernature.figshare.com/articles/figure/Additional_file_13_of_The_GH5_1_4-_-mannanase_from_Bifidobacterium_animalis_subsp_lactis_Bl-04_possesses_a_low-affinity_mannan-binding_module_and_highlights_the_diversity_of_mannanolytic_enzymes/4394894 %R 10.6084/m9.figshare.c.3621353_D1.v1 %2 https://springernature.figshare.com/ndownloader/files/7121261 %K Bifidobacterium %K Carbohydrate-binding module %K Gut microbiota %K Mannan %K Probiotic bacteria %K Surface plasmon resonance %X Multiple sequence alignment of characterized and predicted CBM10 sequences. The list of CBM10 sequences was obtained from the annotation software website dbCAN ( http://csbl.bmb.uga.edu/dbCAN/index.php ) with the exception of the SlMan5A CBM10 sequence which was added manually. The alignment was done with MAFFT 7 and rendered with ESPript 3. The positions corresponding to Cys5, Tyr8, Trp22, Trp24 and Cys36 in the CjXyn10A CBM10 structure [42] are indicated. The four cysteine residues form two disulphide bridges, while Tyr8, Trp22 and Trp24 where shown to mediate binding to insoluble cellulose in the CjXyn10A CBM10. (TIF 20792 kb) %I figshare