Atomistic details of effect of disulfide bond reduction on active site of Phytase B from Aspergillus niger: A MD Study.

ABSTRACT:

Unlabelled

The molecular integrity of the active site of phytases from fungi is critical for maintaining phytase function as efficient catalytic machines. In this study, the molecular dynamics (MD) of two monomers of phytase B from Aspergillus niger, the disulfide intact monomer (NAP) and a monomer with broken disulfide bonds (RAP), were simulated to explore the conformational basis of the loss of catalytic activity when disulfide bonds are broken. The simulations indicated that the overall secondary and tertiary structures of the two monomers were nearly identical but differed in some crucial secondary-structural elements in the vicinity of the disulfide bonds and catalytic site. Disulfide bonds stabilize the β-sheet that contains residue Arg66 of the active site and destabilize t

SUBMITTER: Kumar K 

PROVIDER: S-EPMC3867648 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature