10.1371/journal.pone.0094166.g002
Taichi E. Takasuka
Taichi E.
Takasuka
Justin F. Acheson
Justin F.
Acheson
Christopher M. Bianchetti
Christopher M.
Bianchetti
Ben M. Prom
Ben
M. Prom
Lai F. Bergeman
Lai F.
Bergeman
Adam J. Book
Adam
J. Book
Cameron R. Currie
Cameron R.
Currie
Brian G. Fox
Brian G.
Fox
Schematics of the domain structure in three variants of SACTE_2347.
Public Library of Science
2014
agriculture
Biochemistry
enzymology
Enzyme kinetics
enzymes
Enzyme structure
proteins
Recombinant proteins
glycobiology
proteomics
molecular biology
Molecular biology techniques
Sequencing techniques
Sequence analysis
Energy and power
fuels
biofuels
chemistry
Chemical compounds
Organic compounds
carbohydrates
physics
Condensed matter physics
Solid state physics
crystallography
variants
2014-04-07 03:25:00
Figure
https://plos.figshare.com/articles/figure/_Schematics_of_the_domain_structure_in_three_variants_of_SACTE_2347_/989468
<p>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 <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094166#pone-0094166-t002" target="_blank">Table 2</a> and <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0094166#pone.0094166.s001" target="_blank">Figure S1</a>).</p>