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Enoyl-CoA hydratase

What is it about?

In this study, we report the crystal structure of ECH from Thermus thermophilus HB8 (TtECH) at 2.85 A resolution determined by molecular replacement using RnECH (PDB entry 2dub; Engel et al., 1998) as a search model. Overall, the TtECH monomer assembles into a hexamer similar to that of RnECH with significant structural changes around the active- site region.

Why is it important?

We have crystallized and solved the X-ray structure of ECH from T. thermophilus HB8. ECH is a metabolically important enzyme that is conserved from bacteria to mammals. The structure of TtECH is similar to those of other ECH/ECI members of the Crotonase family.

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Bagautdin Bagautdinov
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