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Publication Abstract from PubMed

Bacillus subtilis BacC is an oxidoreductase involved in the biosynthesis of the potent antibiotic bacilysin. The crystal structure of BacC was determined at 1.19 A resolution. An experimental charge density approach was used to calculate non-covalent interactions within the monomer and across the dimeric interface of BacC. This interaction network, in turn, enabled an analysis of non-covalently connected paths that span the protein structure. One of the pathways of non-covalent interactions was examined by mutational analysis. Biochemical analysis of BacC mutants with potential disruptions in non-covalent interactions along this path revealed that residues that form nodes in pathways of non-covalent interactions influence catalytic activity more than others in a similar chemical environment. Furthermore, we note that nodes in the non-covalent interaction networks are co-localized with compensatory mutation sites identified by multiple sequence alignment of proteins with low sequence similarity to BacC. Put together, this analysis supports the hypothesis that non-covalent nodes represent conserved structural features that can impact the catalytic activity of an enzyme.

Probing the influence of non-covalent contact networks identified by charge density analysis on the oxidoreductase BacC.,Perinbam K, Balaram H, Guru Row TN, Gopal B Protein Eng Des Sel. 2017 Mar 1;30(3):265-272. doi: 10.1093/protein/gzx006. PMID:28158843^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.