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Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase

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Cited 1 time in scopus
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Title
Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase
Other Titles
호냉성 박테리아의 enoyl-CoA isomerase 와 enoyl-CoA hydratase 효소의 구조 및 아미노산 서열 비교
Authors
Hwang, Jisub
Jeong, Chang Sook
Lee, Chang Woo
Shin, Seung Chul
Kim, Han-Woo
Lee, Sung Gu
Youn, Ui Joung
Lee, Chang Sup
Oh, Tae-Jin
Kim, Hak Jun
Park, Hyun
Park, Hyun Ho
Lee, Jun Hyuck
Subject
Microbiology
Keywords
crystal structure; enoyl-CoA isomerase; enoyl- CoA hydratase; X-ray crystallography
Issue Date
2020-07
Citation
Hwang, Jisub, et al. 2020. "Structural and sequence comparisons of bacterial enoyl-CoA isomerase and enoyl-CoA hydratase". JOURNAL OF MICROBIOLOGY, 58(7): 606-613.
Abstract
Crystal structures of enoyl-coenzyme A (CoA) isomerase from Bosea sp. PAMC 26642 (BoECI) and enoyl-CoA hydratase from Hymenobacter sp. PAMC 26628 (HyECH) were determined at 2.35 and 2.70 A resolution, respectively. BoECI and HyECH are members of the crotonase superfamily and are enzymes known to be involved in fatty acid degradation. Structurally, these enzymes are highly similar except for the orientation of their C-terminal helix domain. Analytical ultracentrifugation was performed to determine the oligomerization states of BoECI and HyECH revealing they exist as trimers in solution. However, their putative ligand-binding sites and active site residue compositions are dissimilar. Comparative sequence and structural analysis revealed that the active site of BoECI had one glutamate residue (Glu135), this site is occupied by an aspartate in some ECIs, and the active sites of HyECH had two highly conserved glutamate residues (Glu118 and Glu138). Moreover, HyECH possesses a salt bridge interaction between Glu98 and Arg152 near the active site. This interaction may allow the catalytic Glu118 residue to have a specific conformation for the ECH enzyme reaction. This salt bridge interaction is highly conserved in known bacterial ECH structures and ECI enzymes do not have this type of interaction. Collectively, our comparative sequential and structural studies have provided useful information to distinguish and classify two similar bacterial crotonase superfamily enzymes.
URI
https://repository.kopri.re.kr/handle/201206/12085
DOI
http://dx.doi.org/10.1007/s12275-020-0089-1
Appears in Collections  
2019-2019, Development of potential candidates as antibiotics based on polar genetic resources (19-19) / Lee, Jun Hyuck (PE19210)
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