Conformational Motions and Water Networks at the α/β Interface in E. coli Ribonucleotide Reductase.

ABSTRACT: Ribonucleotide reductases (RNRs) catalyze the conversion of all four ribonucleotides to deoxyribonucleotides and are essential for DNA synthesis in all organisms. The active form of E. coli Ia RNR is composed of two homodimers that form the active α₂β₂ complex. Catalysis is initiated by long-range radical translocation over a ∼32 Å proton-coupled electron transfer (PCET) pathway involving Y356β and Y731α at the interface. Resolving the PCET pathway at the α/β interface has been a long-standing challenge due to the lack of structural data. Herein, molecular dynamics simulations based on a recently solved cryogenic-electron microscopy structure of an active α₂β₂ complex are performed to examine the structure and fluctuations of interfacial w

SUBMITTER: Reinhardt CR 

PROVIDER: S-EPMC7594210 | biostudies-literature | 2020 Aug

REPOSITORIES: biostudies-literature