10.6084/m9.figshare.c.3621353_D1.v1
Johan Morrill
Johan
Morrill
Evelina Kulcinskaja
Evelina
Kulcinskaja
Anna Sulewska
Anna
Sulewska
Sampo Lahtinen
Sampo
Lahtinen
Henrik StĂĽlbrand
Henrik
StĂĽlbrand
Birte Svensson
Birte
Svensson
Maher Abou Hachem
Maher Abou
Hachem
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
Springer Nature
2015
Bifidobacterium
Carbohydrate-binding module
Gut microbiota
Mannan
Probiotic bacteria
Surface plasmon resonance
2015-11-11 05:00:00
Figure
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
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)