TITLE:
The Locus PgaABCD of Acinetobacter junii Putatively Responsible for Poly-β-(1,6)-N-Acetylglucosamine Biosynthesis Might Be Related to Biofilm Formation: A Computational Analysis
AUTHORS:
Bipransh Kumar Tiwary, Arvind Kumar, Ravi Kant Pathak, Nishtha Pandey, Krishna Kant Yadav, Ranadhir Chakraborty
KEYWORDS:
UDP-N-Acetylglucosamine, Glycosyl Transferase, Homology Modeling, Molecular Docking
JOURNAL NAME:
Advances in Microbiology,
Vol.6 No.3,
March
31,
2016
ABSTRACT: Poly-β-(1,6)-N-acetylglucosamine (PNAG),
the chief mediator of intercellular adhesion in many bacteria, plays an important
role in biofilm formation. The pgaABCD
locus was recognized from the whole genome sequence of A. junii SH205. The enzyme glycosyltransferase, PgaC, catalyzes the
production of PNAG with N-acetyl-D-glucosamine monomer. In this study, the possibility
of PNAG biosynthesis in A. junii SH205 with its own PgaC was explored with
the aid of bioinformatics. Multiple alignments of PgaC sequences of different bacteria
were used to identify conserved amino acid residues that might be critical for the
functioning of the protein. Three-dimensional model of A. junii SH205 PgaC was generated for spatial visualization of amino
acid residues. The analyses have shown that the protein PgaC has five conserved
amino acids, Asp140, Asp233,
Gln269, Arg272 and Trp273, critical for
the activity of enzyme. Interaction of UDP-N-acetylglucosamine
within the conserved pocket of glycosyltransferase was explored from molecular docking
studies.