5xg0

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Crystal structure of a novel PET hydrolase from Ideonella sakaiensis 201-F6

Structural highlights

5xg0 is a 3 chain structure with sequence from Ideonella sakaiensis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.58Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PETH_IDESA

Publication Abstract from PubMed

PET hydrolase (PETase), which hydrolyzes polyethylene terephthalate (PET) into soluble building blocks, provides an attractive avenue for the bioconversion of plastics. Here we present the structures of a novel PETase from the PET-consuming microbe Ideonella sakaiensis in complex with substrate and product analogs. Through structural analyses, mutagenesis, and activity measurements, a substrate-binding mode is proposed, and several features critical for catalysis are elucidated.

Structural insight into catalytic mechanism of PET hydrolase.,Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT Nat Commun. 2017 Dec 13;8(1):2106. doi: 10.1038/s41467-017-02255-z. PMID:29235460[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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Citations
27 reviews cite this structure
Enzymatic degradation of plant biomass and synthetic polymers.
Chen et al. (2020)
26 more
80 other articles
No citations found

References

  1. ↑ Han X, Liu W, Huang JW, Ma J, Zheng Y, Ko TP, Xu L, Cheng YS, Chen CC, Guo RT. Structural insight into catalytic mechanism of PET hydrolase. Nat Commun. 2017 Dec 13;8(1):2106. doi: 10.1038/s41467-017-02255-z. PMID:29235460 doi:http://dx.doi.org/10.1038/s41467-017-02255-z

Contents


PDB ID 5xg0

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OCA

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