Allosteric communication in Dihydrofolate Reductase: Signaling network and pathways for closed to occluded transition and back

2007/08/15 by Jie Chen, Chen, Jie, Ruxandra I. Dima +3
Biochemistry, Genetics and Molecular Biology · Materials Science · #Biomolecules (q-bio.BM) #Enzyme Structure and Function #FOS: Biological sciences #Microbial Metabolic Engineering and Bioproduction #Photosynthetic Processes and Mechanisms

paper · pdf · doi:10.48550/arxiv.0708.2083

openalex publication_date 2007/08/15 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/01

Abstract

E. Coli. dihydrofolate reductase (DHFR) undergoes conformational transitions between the closed (CS) and occluded (OS) states which, respectively, describe whether the active site is closed or occluded by the Met20 loop. A sequence-based approach is used to identify a network of residues that represents the allostery wiring diagram. We also use a self-organized polymer model to monitor the kinetics of the CS->OS and the reverse transitions. a sliding motion of Met20 loop is observed. The residues that facilitate the Met20 loop motion are part of the network of residues that transmit allosteric signals during the CS->OS transition.

Citations

• Evolutionarily conserved networks of residues mediate allosteric communication in proteins
• Dynamics of biochemical and biophysical reactions: insight from computer simulations

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