7PZJ

Structure of a bacteroidetal polyethylene terephthalate (PET) esterase

Summary for 7PZJ

• Entry DOI: 10.2210/pdb7pzj/pdb
• Descriptor: Lipase, POTASSIUM ION (3 entities in total)
• Functional Keywords: hydrolases, metagenome, metagenomic screening, pet degradation, polyethylene terephthalate (pet), bacteroidetes, flavobacteriaceae, hydrolase
• Biological source: Chryseobacterium jeonii
• Total number of polymer chains: 1
• Total formula weight: 39067.51

Authors

Zang, H.,Dierkes, R.,Perez-Garcia, P.,Weigert, S.,Sternagel, S.,Hallam, S.J.,Applegate, V.,Schumacher, J.,Schott, T.,Pleiss, J.,Almeida, A.,Hoecker, B.,Smits, S.H.,Schmitz, R.A.,Chow, J.,Streit, W.R. (deposition date: 2021-10-12, release date: 2022-03-02, Last modification date: 2024-10-16)

Primary citation

Zhang, H.,Perez-Garcia, P.,Dierkes, R.F.,Applegate, V.,Schumacher, J.,Chibani, C.M.,Sternagel, S.,Preuss, L.,Weigert, S.,Schmeisser, C.,Danso, D.,Pleiss, J.,Almeida, A.,Hocker, B.,Hallam, S.J.,Schmitz, R.A.,Smits, S.H.J.,Chow, J.,Streit, W.R.
The Bacteroidetes Aequorivita sp. and Kaistella jeonii Produce Promiscuous Esterases With PET-Hydrolyzing Activity.
Front Microbiol, 12:803896-803896, 2021

PubMed Abstract: Certain members of the Actinobacteria and Proteobacteria are known to degrade polyethylene terephthalate (PET). Here, we describe the first functional PET-active enzymes from the Bacteroidetes phylum. Using a PETase-specific Hidden-Markov-Model- (HMM-) based search algorithm, we identified several PETase candidates from Flavobacteriaceae and Porphyromonadaceae. Among them, two promiscuous and cold-active esterases derived from sp. (PET27) and (PET30) showed depolymerizing activity on polycaprolactone (PCL), amorphous PET foil and on the polyester polyurethane Impranil DLN. PET27 is a 37.8 kDa enzyme that released an average of 174.4 nmol terephthalic acid (TPA) after 120 h at 30°C from a 7 mg PET foil platelet in a 200 μl reaction volume, 38-times more than PET30 (37.4 kDa) released under the same conditions. The crystal structure of PET30 without its C-terminal Por-domain (PET30ΔPorC) was solved at 2.1 Å and displays high structural similarity to the PETase. PET30 shows a Phe-Met-Tyr substrate binding motif, which seems to be a unique feature, as PETase, LCC and PET2 all contain Tyr-Met-Trp binding residues, while PET27 possesses a Phe-Met-Trp motif that is identical to Cut190. Microscopic analyses showed that cells are indeed able to bind on and colonize PET surfaces after a few days of incubation. Homologs of PET27 and PET30 were detected in metagenomes, predominantly aquatic habitats, encompassing a wide range of different global climate zones and suggesting a hitherto unknown influence of this bacterial phylum on man-made polymer degradation.

PubMed: 35069509
DOI: 10.3389/fmicb.2021.803896

Experimental method

X-RAY DIFFRACTION (2.1 Å)