7DZU

Cyrstal structure of PETase K169A mutant from Rhizobacter gummiphilus

7DZU の概要

• エントリーDOI: 10.2210/pdb7dzu/pdb
• 分子名称: DLH domain-containing protein (2 entities in total)
• 機能のキーワード: pet hydrolase, hydrolase
• 由来する生物種: Rhizobacter gummiphilus (Methylibium sp. NS21)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 28478.61

構造登録者

Sagong, H.-Y.,Kim, K.-J. (登録日: 2021-01-26, 公開日: 2021-07-07, 最終更新日: 2024-10-23)

主引用文献

Sagong, H.Y.,Son, H.F.,Seo, H.,Hong, H.,Lee, D.,Kim, K.J.
Implications for the PET decomposition mechanism through similarity and dissimilarity between PETases from Rhizobacter gummiphilus and Ideonella sakaiensis.
J Hazard Mater, 416:126075-126075, 2021

PubMed Abstract: The development of a superb polyethylene terephthalate (PET) hydrolyzing enzyme requires an accurate understanding of the PET decomposition mechanism. However, studies on PET degrading enzymes, including the PET hydrolase from Ideonella sakaiensis (IsPETase), have not provided sufficient knowledge of the molecular mechanisms for the hardly accessible substrate. Here, we report a novel PET hydrolase from Rhizobacter gummiphilus (RgPETase), which has a hydrolyzing activity similar to IsPETase toward microcrystalline PET but distinct behavior toward low crystallinity PET film. Structural analysis of RgPETase reveals that the enzyme shares the key structural features of IsPETase for high PET hydrolysis activity but has distinguished structures at the surface-exposed regions. RgPETase shows a unique conformation of the wobbling tryptophan containing loop (WW-loop) and change of the electrostatic surface charge on the loop dramatically affects the PET-degrading activity. We further show that effect of the electrostatic surface charge to the activity varies depending on locations. This work provides valuable information underlying the uncovered PET decomposition mechanism.

PubMed: 34492896
DOI: 10.1016/j.jhazmat.2021.126075

実験手法

X-RAY DIFFRACTION (2.4 Å)