1UIY
Crystal Structure of Enoyl-CoA Hydratase from Thermus Thermophilus HB8
Summary for 1UIY
| Entry DOI | 10.2210/pdb1uiy/pdb |
| Descriptor | Enoyl-CoA Hydratase, 1,4-DIETHYLENE DIOXIDE, GLYCEROL, ... (4 entities in total) |
| Functional Keywords | lyase, beta-oxidation, crotonase, coa, riken structural genomics/proteomics initiative, rsgi, structural genomics |
| Biological source | Thermus thermophilus |
| Total number of polymer chains | 1 |
| Total formula weight | 27628.24 |
| Authors | Bagautdinov, B.,Kuramitsu, S.,Yokoyama, S.,Miyano, M.,Tahirov, T.H.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2003-07-24, release date: 2003-08-05, Last modification date: 2024-11-20) |
| Primary citation | 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 Cited by 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: 33949975DOI: 10.1107/S2053230X21004593 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.85 Å) |
Structure validation
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