KMID : 1094720190240010155
|
|
Biotechnology and Bioprocess Engineering 2019 Volume.24 No. 1 p.155 ~ p.162
|
|
Crystal Structure of a Novel Type Isomerase of Enoyl-CoA Hydratase/Isomerase Family Protein from Cupriavidus necator H16
|
|
Seo Ho-Gyun
Kim Kyung-Jin
|
|
Abstract
|
|
|
Although enoyl-CoA hydratase/isomerase superfamily proteins are functionally diverse and extremely abundant in microbial and higher organism¡¯s genome, they still have been elusively annotated. The genome of Cupriavidus necator H16 contains at least 54 enoyl-CoA hydratase/isomerase superfamily proteins that might influence on polyhydroxyalkanoate synthesis, but most of them are uncharacterized. Among them, we first determined crystal structure of H16_B0756 at a 2.0 A resolution. The protein exhibits unique amino acid sequences compared to the other isoforms with identity lower than 36%. The structure of H16_B0756 forms a trimeric architecture and showed canonical disk-shape. Interestingly, H16_B0756 has only one glutamate residue at the active site while other enoyl-CoA hydratases have two nucleophilic glutamate at the catalytic site. We found that the active site conformation of H16_B0756 is quite similar to that of 1,2-epoxyphenylacetyl-CoA isomerase (PaaG) rather than those of other enoyl-CoA hydratases. In addition to the structural comparison, gene neighborhoods analysis suggested that H16_B0756 might function in the ring compound degradation.
|
|
KEYWORD
|
|
crotonase superfamily, H16_B0756, Cupriavidus necator H16, ring compound degradation, polyhydroxyalkanoate
|
|
FullTexts / Linksout information
|
|
|
|
Listed journal information
|
|
|