6SCD
Polyester hydrolase PE-H Y250S mutant of Pseudomonas aestusnigri
Summary for 6SCD
| Entry DOI | 10.2210/pdb6scd/pdb |
| Related | 6SBN |
| Descriptor | Polyester hydrolase, SULFATE ION, PHOSPHATE ION, ... (9 entities in total) |
| Functional Keywords | polyester degradation, pet hydrolase, marine bacteria, pseudomonas aestusnigri, hydrolase |
| Biological source | Pseudomonas aestusnigri |
| Total number of polymer chains | 2 |
| Total formula weight | 67563.75 |
| Authors | Bollinger, A.,Thies, S.,Kobus, S.,Hoeppner, A.,Smits, S.H.J.,Jaeger, K.-E. (deposition date: 2019-07-24, release date: 2020-02-26, Last modification date: 2024-11-20) |
| Primary citation | Bollinger, A.,Thies, S.,Knieps-Grunhagen, E.,Gertzen, C.,Kobus, S.,Hoppner, A.,Ferrer, M.,Gohlke, H.,Smits, S.H.J.,Jaeger, K.E. A Novel Polyester Hydrolase From the Marine BacteriumPseudomonas aestusnigri -Structural and Functional Insights. Front Microbiol, 11:114-114, 2020 Cited by PubMed Abstract: Biodegradation of synthetic polymers, in particular polyethylene terephthalate (PET), is of great importance, since environmental pollution with PET and other plastics has become a severe global problem. Here, we report on the polyester degrading ability of a novel carboxylic ester hydrolase identified in the genome of the marine hydrocarbonoclastic bacterium VGXO14 . The enzyme, designated PE-H, belongs to the type IIa family of PET hydrolytic enzymes as indicated by amino acid sequence homology. It was produced in , purified and its crystal structure was solved at 1.09 Å resolution representing the first structure of a type IIa PET hydrolytic enzyme. The structure shows a typical α/β-hydrolase fold and high structural homology to known polyester hydrolases. PET hydrolysis was detected at 30°C with amorphous PET film (PETa), but not with PET film from a commercial PET bottle (PETb). A rational mutagenesis study to improve the PET degrading potential of PE-H yielded variant PE-H (Y250S) which showed improved activity, ultimately also allowing the hydrolysis of PETb. The crystal structure of this variant solved at 1.35 Å resolution allowed to rationalize the improvement of enzymatic activity. A PET oligomer binding model was proposed by molecular docking computations. Our results indicate a significant potential of the marine bacterium for PET degradation. PubMed: 32117139DOI: 10.3389/fmicb.2020.00114 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.35 Å) |
Structure validation
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