| Full text | |
| Author(s): Show less - |
Austin, Harry P.
[1]
;
Allen, Mark D.
[1]
;
Donohoe, Bryon S.
[2]
;
Rorrer, Nicholas A.
[3]
;
Kearns, Fiona L.
[4]
;
Silveira, Rodrigo L.
[5, 2]
;
Pollard, Benjamin C.
[4]
;
Dominick, Graham
[3]
;
Duman, Ramona
[6]
;
El Omari, Kamel
[6]
;
Mykhaylyk, Vitaliy
[6]
;
Wagner, Armin
[6]
;
Michener, William E.
[3]
;
Amore, Antonella
[2]
;
Skaf, Munir S.
[5]
;
Crowley, Michael F.
[2]
;
Thorne, Alan W.
[1]
;
Johnson, Christopher W.
[3]
;
Woodcock, H. Lee
[4]
;
McGeehan, John E.
[1]
;
Beckham, Gregg T.
[3]
Total Authors: 21
|
| Affiliation: | [1] Univ Portsmouth, Inst Biol & Biomed Sci, Sch Biol Sci, Mol Biophys Labs, Portsmouth PO1 2DY, Hants - England
[2] Natl Renewable Energy Lab, Biosci Ctr, Golden, CO 80401 - USA
[3] Natl Renewable Energy Lab, Natl Bioenergy Ctr, Golden, CO 80401 - USA
[4] Univ S Florida, Dept Chem, Tampa, FL 33620 - USA
[5] Univ Estadual Campinas, Inst Chem, BR-13083970 Campinas, SP - Brazil
[6] Harwell Sci & Innovat Campus, Diamond Light Source, Didcot OX11 0DE, Oxon - England
Total Affiliations: 6
|
| Document type: | Journal article |
| Source: | PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA; v. 115, n. 19, p. E4350-E4357, MAY 8 2018. |
| Web of Science Citations: | 67 |
| 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 angstrom resolution X-ray crystal structure of PETase, which reveals features common to both cutinases and lipases. PETase retains the ancestral alpha/beta-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. (AU) | |
| FAPESP's process: | 13/08293-7 - CCES - Center for Computational Engineering and Sciences |
| Grantee: | Munir Salomao Skaf |
| Support Opportunities: | Research Grants - Research, Innovation and Dissemination Centers - RIDC |
| FAPESP's process: | 14/10448-1 - Molecular aspects of plant cell wall architecture |
| Grantee: | Rodrigo Leandro Silveira |
| Support Opportunities: | Scholarships in Brazil - Post-Doctoral |
| FAPESP's process: | 16/22956-7 - Hybrid QM/MM simulations of feruloyl esterases: cleavage mechanism of lignin-carbohydrate complexes in plant cell walls |
| Grantee: | Rodrigo Leandro Silveira |
| Support Opportunities: | Scholarships abroad - Research Internship - Post-doctor |