1UIY

Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8

1UIY の概要

• エントリーDOI: 10.2210/pdb1uiy/pdb
• 分子名称: Enoyl-CoA Hydratase, 1,4-DIETHYLENE DIOXIDE, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: lyase, beta-oxidation, crotonase, coa, riken structural genomics/proteomics initiative, rsgi, structural genomics
• 由来する生物種: Thermus thermophilus
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 27628.24

構造登録者

Bagautdinov, B.,Kuramitsu, S.,Yokoyama, S.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2003-07-24, 公開日: 2003-08-05, 最終更新日: 2024-11-20)

主引用文献

Padavattan, S.,Jos, S.,Gogoi, H.,Bagautdinov, B.
Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.
Acta Crystallogr.,Sect.F, 77:148-155, 2021

PubMed Abstract: Fatty-acid degradation is an oxidative process that involves four enzymatic steps and is referred to as the β-oxidation pathway. During this process, long-chain acyl-CoAs are broken down into acetyl-CoA, which enters the mitochondrial tricarboxylic acid (TCA) cycle, resulting in the production of energy in the form of ATP. Enoyl-CoA hydratase (ECH) catalyzes the second step of the β-oxidation pathway by the syn addition of water to the double bond between C2 and C3 of a 2-trans-enoyl-CoA, resulting in the formation of a 3-hydroxyacyl CoA. Here, the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) is reported at 2.85 Å resolution. TtECH forms a hexamer as a dimer of trimers, and wide clefts are uniquely formed between the two trimers. Although the overall structure of TtECH is similar to that of a hexameric ECH from Rattus norvegicus (RnECH), there is a significant shift in the positions of the helices and loops around the active-site region, which includes the replacement of a longer α3 helix with a shorter α-helix and 3-helix in RnECH. Additionally, one of the catalytic residues of RnECH, Glu144 (numbering based on the RnECH enzyme), is replaced by a glycine in TtECH, while the other catalytic residue Glu164, as well as Ala98 and Gly141 that stabilize the enolate intermediate, is conserved. Their putative ligand-binding sites and active-site residue compositions are dissimilar.

PubMed: 33949975
DOI: 10.1107/S2053230X21004593

実験手法

X-RAY DIFFRACTION (2.85 Å)