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Characterization and engineering of a plastic-degrading aromatic polyesterase

Overview of attention for article published in Proceedings of the National Academy of Sciences of the United States of America, April 2018
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About this Attention Score

  • In the top 5% of all research outputs scored by Altmetric
  • Among the highest-scoring outputs from this source (#40 of 80,050)
  • High Attention Score compared to outputs of the same age (99th percentile)
  • High Attention Score compared to outputs of the same age and source (99th percentile)

Citations

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46 Dimensions

Readers on

mendeley
729 Mendeley
citeulike
1 CiteULike
Title
Characterization and engineering of a plastic-degrading aromatic polyesterase
Published in
Proceedings of the National Academy of Sciences of the United States of America, April 2018
DOI 10.1073/pnas.1718804115
Pubmed ID
Authors

Harry P. Austin, Mark D. Allen, Bryon S. Donohoe, Nicholas A. Rorrer, Fiona L. Kearns, Rodrigo L. Silveira, Benjamin C. Pollard, Graham Dominick, Ramona Duman, Kamel El Omari, Vitaliy Mykhaylyk, Armin Wagner, William E. Michener, Antonella Amore, Munir S. Skaf, Michael F. Crowley, Alan W. Thorne, Christopher W. Johnson, H. Lee Woodcock, John E. McGeehan, Gregg T. Beckham

Abstract

Poly(ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers and is accumulating in the environment at a staggering rate as discarded packaging and textiles. The properties that make PET so useful also endow it with an alarming resistance to biodegradation, likely lasting centuries in the environment. Our collective reliance on PET and other plastics means that this buildup will continue unless solutions are found. Recently, a newly discovered bacterium, Ideonella sakaiensis 201-F6, was shown to exhibit the rare ability to grow on PET as a major carbon and energy source. Central to its PET biodegradation capability is a secreted PETase (PET-digesting enzyme). Here, we present a 0.92 Å resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral α/β-hydrolase fold but exhibits a more open active-site cleft than homologous cutinases. By narrowing the binding cleft via mutation of two active-site residues to conserved amino acids in cutinases, we surprisingly observe improved PET degradation, suggesting that PETase is not fully optimized for crystalline PET degradation, despite presumably evolving in a PET-rich environment. Additionally, we show that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties. In contrast, PETase does not degrade aliphatic polyesters, suggesting that it is generally an aromatic polyesterase. These findings suggest that additional protein engineering to increase PETase performance is realistic and highlight the need for further developments of structure/activity relationships for biodegradation of synthetic polyesters.

Twitter Demographics

The data shown below were collected from the profiles of 277 tweeters who shared this research output. Click here to find out more about how the information was compiled.

Mendeley readers

The data shown below were compiled from readership statistics for 729 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Unknown 729 100%

Demographic breakdown

Readers by professional status Count As %
Student > Bachelor 181 25%
Student > Ph. D. Student 121 17%
Researcher 114 16%
Student > Master 106 15%
Unspecified 102 14%
Other 127 17%
Readers by discipline Count As %
Biochemistry, Genetics and Molecular Biology 209 29%
Unspecified 136 19%
Agricultural and Biological Sciences 135 19%
Chemistry 90 12%
Engineering 50 7%
Other 131 18%

Attention Score in Context

This research output has an Altmetric Attention Score of 2110. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 01 August 2019.
All research outputs
#683
of 13,384,641 outputs
Outputs from Proceedings of the National Academy of Sciences of the United States of America
#40
of 80,050 outputs
Outputs of similar age
#37
of 270,603 outputs
Outputs of similar age from Proceedings of the National Academy of Sciences of the United States of America
#3
of 1,009 outputs
Altmetric has tracked 13,384,641 research outputs across all sources so far. Compared to these this one has done particularly well and is in the 99th percentile: it's in the top 5% of all research outputs ever tracked by Altmetric.
So far Altmetric has tracked 80,050 research outputs from this source. They typically receive a lot more attention than average, with a mean Attention Score of 23.9. This one has done particularly well, scoring higher than 99% of its peers.
Older research outputs will score higher simply because they've had more time to accumulate mentions. To account for age we can compare this Altmetric Attention Score to the 270,603 tracked outputs that were published within six weeks on either side of this one in any source. This one has done particularly well, scoring higher than 99% of its contemporaries.
We're also able to compare this research output to 1,009 others from the same source and published within six weeks on either side of this one. This one has done particularly well, scoring higher than 99% of its contemporaries.