Skip to main content
Scientific Reports logoLink to Scientific Reports
. 2020 Apr 8;10:6287. doi: 10.1038/s41598-020-62786-2

Author Correction: Structural Features of a Bacteroidetes-Affiliated Cellulase Linked with a Polysaccharide Utilization Locus

A E Naas 1,, A K MacKenzie 1, B Dalhus 2,3, V G H Eijsink 1, P B Pope 1,
PMCID: PMC7142078  PMID: 32269252

Correction to: Scientific Reports 10.1038/srep11666, published online 02 July 2015

This Article contains an error, where the protein name corresponding to 4IM4 (pdbid) is incorrectly given as “Lic26A-Cel5E”, and should read “CelE”.

In addition, three references were omitted from Table 2, and are given below as References 13.

The correct Table 2 and Figure 4 are given below as Table 1 and Figure 1 respectively.

Table 1.

Structural comparison of AC2aCel5A with its six closest structural homologues identified using the DALI server17, along with reported enzyme activities.

Structural comparison Enzymatic activities Reference
DALI Z-score RMSD (Å) % id CMC (U/mg) β-glucan (U/mg) Filter paper (U/mg) Avicel (U/mg) Lichenan (U/mg) Xylan (U/mg) Xyloglucan (U/mg)
Bacteroidetes AC2a Cellulase Cel5A 216.8 1471.4 0.152a 0.115a 839.9 nd trace This study and7
Paenibacillus pabuli Xyloglucanase XG5 (2JEP) 49.2 1.6 34 nd nd nd nd nd 8700 33
Clostridium cellulovorans Cellulase EngD (3NDY) 47.0 1.7 33 15 42 0.017 0.5 36 15
Bacteroides ovatus Xyloglucanase BoGH5A (3ZMR) 46.6 1.9 32 nd nd nd 514.2 44
Clostridium thermocellum Cellulase CelE (4IM4) 46.0 1.6 32 Active 75.4 Active Active 13, b
Clostridium cellulolyticum Cellulase CelCCA (1EDG) 45.9 1.9 32 101.3 104.3 0.028 (0.124)d 79.2 10.1 45,46, c
Piromyces rhizinflata Cellulase CelAcd (3AYR) 43.2 1.8 30 344.9 576 0.64 1.39 542.5 106.2 47

RMSD; root-mean-square deviation of C-alpha atoms. The structural homologues are sorted based on the Z-score obtained in the DALI search. One Unit of enzyme activity was defined as the amount of enzyme releasing 1 µmol of reducing sugar equivalents per minute. “nd” means not detected, whereas a hyphen, “—”, indicates “not tested”.

aµmol reducing sugar equivalents calculated as µmol cellotriose + µmol cellobiose + µmol glucose, quantified by HPAEC-PAD7.

bGH5 domain of CelE.

cU/mg calculated from U/µmol reported in45.

dFor this enzyme data for both the full length protein (in parentheses), and the catalytic domain only were published.

Figure 1.

Figure 1

.

Finally, the updated Supplementary Information file, containing the correct protein name in Figure S1, is given below.

Supplementary information

Contributor Information

A. E. Naas, Email: adrian.naas@nmbu.no

P. B. Pope, Email: phil.pope@nmbu.no

Supplementary information

is available for this paper at 10.1038/s41598-020-62786-2.

References

  • 1.Hall J, Hazlewood GP, Barker PJ, Gilbert HJ. Conserved reiterated domains in Clostridium thermocellum endoglucanases. Gene. 1988;69:29–38. doi: 10.1016/0378-1119(88)90375-7. [DOI] [PubMed] [Google Scholar]
  • 2.Durrant AJ, Hall J, Hazlewoodt GP, Gilbert HJ. The non-catalytic C-terminal region of endoglucanase E from Clostridium thermocellum contains a cellulose-binding domain. Biochem. J. 1991;273:289–293. doi: 10.1042/bj2730289. [DOI] [PMC free article] [PubMed] [Google Scholar]
  • 3.Takasuka TE, et al. Cell-free translation of biofuel enzymes. Methods Mol. Biol. 2014;1118:71–95. doi: 10.1007/978-1-62703-782-2_5. [DOI] [PMC free article] [PubMed] [Google Scholar]

Associated Data

This section collects any data citations, data availability statements, or supplementary materials included in this article.

Supplementary Materials


Articles from Scientific Reports are provided here courtesy of Nature Publishing Group

RESOURCES