Structural insights into E. coli porphobilinogen deaminase during synthesis and exit of 1-hydroxymethylbilane.

ABSTRACT: Porphobilinogen deaminase (PBGD) catalyzes the formation of 1-hydroxymethylbilane (HMB), a crucial intermediate in tetrapyrrole biosynthesis, through a step-wise polymerization of four molecules of porphobilinogen (PBG), using a unique dipyrromethane (DPM) cofactor. Structural and biochemical studies have suggested residues with catalytic importance, but their specific role in the mechanism and the dynamic behavior of the protein with respect to the growing pyrrole chain remains unknown. Molecular dynamics simulations of the protein through the different stages of pyrrole chain elongation suggested that the compactness of the overall protein decreases progressively with addition of each pyrrole ring. Essential dynamics showed that domains move apart while the cofactor turn region moves tow

SUBMITTER: Bung N 

PROVIDER: S-EPMC3945110 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature