Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8.
Thermus thermophilus HB8
crotonases
crystal structure
enoyl-CoA hydratase
fatty-acid metabolism
β-oxidation pathway
Journal
Acta crystallographica. Section F, Structural biology communications
ISSN: 2053-230X
Titre abrégé: Acta Crystallogr F Struct Biol Commun
Pays: United States
ID NLM: 101620319
Informations de publication
Date de publication:
01 May 2021
01 May 2021
Historique:
received:
03
03
2021
accepted:
30
04
2021
entrez:
5
5
2021
pubmed:
6
5
2021
medline:
23
11
2021
Statut:
ppublish
Résumé
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
Identifiants
pubmed: 33949975
pii: S2053230X21004593
doi: 10.1107/S2053230X21004593
pmc: PMC8098125
doi:
Substances chimiques
Enoyl-CoA Hydratase
EC 4.2.1.17
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
148-155Références
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