6EQF

Crystal structure of a polyethylene terephthalate degrading hydrolase from Ideonella sakaiensis in spacegroup P212121

6EQF の概要

• エントリーDOI: 10.2210/pdb6eqf/pdb
• 関連するPDBエントリー: 6EQD
• 分子名称: Poly(ethylene terephthalate) hydrolase, CHLORIDE ION (3 entities in total)
• 機能のキーワード: petase, pet degradation, a/b hydrolase, hydrolase
• 由来する生物種: Ideonella sakaiensis
• 細胞内の位置: Secreted : A0A0K8P6T7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31377.38

構造登録者

Austin, H.P.,Allen, M.D.,Johnson, C.W.,Beckham, G.T.,McGeehan, J.E. (登録日: 2017-10-12, 公開日: 2018-04-25, 最終更新日: 2024-11-20)

主引用文献

Austin, H.P.,Allen, M.D.,Donohoe, B.S.,Rorrer, N.A.,Kearns, F.L.,Silveira, R.L.,Pollard, B.C.,Dominick, G.,Duman, R.,El Omari, K.,Mykhaylyk, V.,Wagner, A.,Michener, W.E.,Amore, A.,Skaf, M.S.,Crowley, M.F.,Thorne, A.W.,Johnson, C.W.,Woodcock, H.L.,McGeehan, J.E.,Beckham, G.T.
Characterization and engineering of a plastic-degrading aromatic polyesterase.
Proc. Natl. Acad. Sci. U.S.A., 115:E4350-E4357, 2018

PubMed 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, 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.

PubMed: 29666242
DOI: 10.1073/pnas.1718804115

実験手法

X-RAY DIFFRACTION (1.7 Å)