8AIT
Crystal structure of cutinase PbauzCut from Pseudomonas bauzanensis
Summary for 8AIT
| Entry DOI | 10.2210/pdb8ait/pdb |
| Descriptor | Cutinase, SULFATE ION (3 entities in total) |
| Functional Keywords | cutinase, ester bond, cleavage, pet, hydrolase |
| Biological source | Halopseudomonas bauzanensis |
| Total number of polymer chains | 1 |
| Total formula weight | 33874.58 |
| Authors | Zahn, M.,Allen, M.D.,Pickford, A.R.,McGeehan, J.E. (deposition date: 2022-07-27, release date: 2023-03-08, Last modification date: 2024-02-07) |
| Primary citation | Avilan, L.,Lichtenstein, B.R.,Konig, G.,Zahn, M.,Allen, M.D.,Oliveira, L.,Clark, M.,Bemmer, V.,Graham, R.,Austin, H.P.,Dominick, G.,Johnson, C.W.,Beckham, G.T.,McGeehan, J.E.,Pickford, A.R. Concentration-Dependent Inhibition of Mesophilic PETases on Poly(ethylene terephthalate) Can Be Eliminated by Enzyme Engineering. ChemSusChem, 16:e202202277-e202202277, 2023 Cited by PubMed Abstract: Enzyme-based depolymerization is a viable approach for recycling of poly(ethylene terephthalate) (PET). PETase from Ideonella sakaiensis (IsPETase) is capable of PET hydrolysis under mild conditions but suffers from concentration-dependent inhibition. In this study, this inhibition is found to be dependent on incubation time, the solution conditions, and PET surface area. Furthermore, this inhibition is evident in other mesophilic PET-degrading enzymes to varying degrees, independent of the level of PET depolymerization activity. The inhibition has no clear structural basis, but moderately thermostable IsPETase variants exhibit reduced inhibition, and the property is completely absent in the highly thermostable HotPETase, previously engineered by directed evolution, which simulations suggest results from reduced flexibility around the active site. This work highlights a limitation in applying natural mesophilic hydrolases for PET hydrolysis and reveals an unexpected positive outcome of engineering these enzymes for enhanced thermostability. PubMed: 36811288DOI: 10.1002/cssc.202202277 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.24 Å) |
Structure validation
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