Thermal activation of 'allosteric-like' large-scale motions in a eukaryotic Lactate Dehydrogenase.

ABSTRACT: Conformational changes occurring during the enzymatic turnover are essential for the regulation of protein functionality. Individuating the protein regions involved in these changes and the associated mechanical modes is still a challenge at both experimental and theoretical levels. We present here a detailed investigation of the thermal activation of the functional modes and conformational changes in a eukaryotic Lactate Dehydrogenase enzyme (LDH). Neutron Spin Echo spectroscopy and Molecular Dynamics simulations were used to uncover the characteristic length- and timescales of the LDH nanoscale motions in the apo state. The modes involving the catalytic loop and the mobile region around the binding site are activated at room temperature, and match the allosteric reorganisation of bacteri

SUBMITTER: Katava M 

PROVIDER: S-EPMC5253740 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature