Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst

@inproceedings{Warden2015RationalEO,
  title={Rational engineering of a mesohalophilic carbonic anhydrase to an extreme halotolerant biocatalyst},
  author={Andrew C Warden and Michelle Williams and Thomas S. Peat and Shane A. Seabrook and Janet Newman and Greg Dojchinov and Victoria S Haritos},
  booktitle={Nature communications},
  year={2015}
}
Enzymes expressed by highly salt-tolerant organisms show many modifications compared with salt-affected counterparts including biased amino acid and lower α-helix content, lower solvent accessibility and negative surface charge. Here, we show that halotolerance can be generated in an enzyme solely by modifying surface residues. Rational design of carbonic anhydrase II is undertaken in three stages replacing 18 residues in total, crystal structures confirm changes are confined to surface… CONTINUE READING
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Coordinates and structure factors for M1, M2, M3 and M4 have been deposited in the RCSB Protein Data Bank under accession codes 4CNR, 4CNV, 4CNW and 4CNX, respectively

Phan, D. T. et al. A study of bovine, +21 authors prepared the manuscript. Additional information Accession codes
Supplementary Information accompanies this paper at http://www.nature.com/ naturecommunications Competing financial interests: The authors declare no competing financial interests. Reprints and permission information is available online at http://npg.nature.com/ reprintsandpermissions/ How to cite t • 2015

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