Molecular dynamics studies unravel role of conserved residues responsible for movement of ions into active site of DHBPS.

ABSTRACT: 3,4-dihydroxy-2-butanone-4-phosphate synthase (DHBPS) catalyzes the conversion of D-ribulose 5-phosphate (Ru5P) to L-3,4-dihydroxy-2-butanone-4-phosphate in the presence of Mg²⁺. Although crystal structures of DHBPS in complex with Ru5P and non-catalytic metal ions have been reported, structure with Ru5P along with Mg²⁺ is still elusive. Therefore, mechanistic role played by Mg²⁺ in the structure of DHBPS is poorly understood. In this study, molecular dynamics simulations of DHBPS-Ru5P complex along with Mg²⁺ have shown entry of Mg²⁺ from bulk solvent into active site. Presence of Mg²⁺ in active site has constrained conformations of Ru5P and has reduced flexibility of loop-2. Formation of hydrogen bonds among Thr-108 and res

SUBMITTER: Shinde RN 

PROVIDER: S-EPMC5228156 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature