%0 Figure %A Takasuka, Taichi E. %A Acheson, Justin F. %A Bianchetti, Christopher M. %A M. Prom, Ben %A Bergeman, Lai F. %A J. Book, Adam %A Currie, Cameron R. %A Fox, Brian G. %D 2014 %T Schematics of the domain structure in three variants of SACTE_2347. %U https://plos.figshare.com/articles/figure/_Schematics_of_the_domain_structure_in_three_variants_of_SACTE_2347_/989468 %R 10.1371/journal.pone.0094166.g002 %2 https://plos.figshare.com/ndownloader/files/1452931 %K agriculture %K Biochemistry %K enzymology %K Enzyme kinetics %K enzymes %K Enzyme structure %K proteins %K Recombinant proteins %K glycobiology %K proteomics %K molecular biology %K Molecular biology techniques %K Sequencing techniques %K Sequence analysis %K Energy and power %K fuels %K biofuels %K chemistry %K Chemical compounds %K Organic compounds %K carbohydrates %K physics %K Condensed matter physics %K Solid state physics %K crystallography %K variants %X

A, SACTE_2347_FL; B, SACTE_2347_42kDa; C, SACTE_2347_34kDa. Residues 1–41 correspond to the annotated twin arginine translocation peptide. Residue 51 corresponds to the experimentally determined N-terminus in the three variants. The GH5 domain spans residues 63–308, and boundaries of the Fn3 and CBM2 domains are as indicated. The location of C-terminal tryptic-digest polypeptides for each variant is shown (GH5, 34kDa-C, Fn3, 42kDa-C, CBM2; also shown in Table 2 and Figure S1).

%I PLOS ONE