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.
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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.
Perspectives
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. TtECH has only one conserved glutamate residue in the catalytic site, mimicking a monofunctional enzyme with ECI activity.
Dr Bagautdin Bagautdinov
Read the Original
This page is a summary of: Crystal structure of enoyl-CoA hydratase from Thermus thermophilus HB8, Acta Crystallographica Section F Structural Biology Communications, May 2021, International Union of Crystallography,
DOI: 10.1107/s2053230x21004593.
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