Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)Crystal structure of a cutinase enzyme from Thermobifida fusca YX (705)

Structural highlights

7qjs is a 2 chain structure with sequence from Thermobifida fusca YX. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 1.429Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PETH1_THEFY Catalyzes the hydrolysis of cutin, a polyester that forms the structure of plant cuticle (PubMed:18658138). Shows esterase activity towards p-nitrophenol-linked aliphatic esters (pNP-aliphatic esters) (PubMed:18658138, PubMed:25545638). Also hydrolyzes the triglyceride triolein (PubMed:18658138). Capable of degrading the plastic poly(ethylene terephthalate) (PET), the most abundant polyester plastic in the world (PubMed:25545638).[1] [2]

References

  1. Chen S, Tong X, Woodard RW, Du G, Wu J, Chen J. Identification and characterization of bacterial cutinase. J Biol Chem. 2008 Sep 19;283(38):25854-62. PMID:18658138 doi:10.1074/jbc.M800848200
  2. Then J, Wei R, Oeser T, Barth M, Belisario-Ferrari MR, Schmidt J, Zimmermann W. Ca2+ and Mg2+ binding site engineering increases the degradation of polyethylene terephthalate films by polyester hydrolases from Thermobifida fusca. Biotechnol J. 2015 Apr;10(4):592-8. doi: 10.1002/biot.201400620. Epub 2015 Jan, 19. PMID:25545638 doi:http://dx.doi.org/10.1002/biot.201400620

7qjs, resolution 1.43Å

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