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 ?-sheet that contains residue Arg66 of the active site and destabilize the ?-helix that contains the catalytic residue Asp319. This stabilization and destabilization lead to changes in the shape of the active-site pocket. Functionally important hydrogen bonds and atomic fluctuations in the catalytic pocket change during the RAP simulation. None of the disulfide bonds are in or near the catalytic pocket but are most likely essential for maintaining the native conformation of the catalytic site. ABBREVIATIONS:PhyB - 2.5 pH acid phophatese from Aspergillus niger, NAP - disulphide intact monomer of Phytase B, RAP - disulphide reduced monomer of Phytase B, Rg - radius of gyration, RMSD - root mean square deviation, MD - molecular dynamics.

SUBMITTER: Kumar K 

PROVIDER: S-EPMC3867648 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature