Design and construction of a structural model of the bifunctional GlmU protein in complex with N‐acetyl‐D‐glucosamine‐1‐phosphate and uridine‐diphosphate‐N‐acetylglucosamine

Abstract

The focus of this project was to explore the structure of the GlmU protein from E. coli (PDB ID: 2OI7) and to design and build a physical model that illustrates the key functional features of the protein. GlmU is a bifunctional bacterial protein that synthesizes uridine‐diphosphate‐N‐acetylglucosamine (UDP‐GlcNAc) from D‐glucosamine 1‐phosphate, acetyl‐CoA, and UTP. The structure described here is in complex with the products desulfo‐coenzyme A, N‐acetyl‐D‐glucosamine‐1‐phosphate and UDP‐GlcNAc. The N‐terminal uridyltransferase domain is composed of two beta‐hairpins and a seven‐stranded beta‐sheet surrounded by alpha‐helices. The C‐terminal acetyltransferase domain is a left‐handed parallel beta‐helix. GlmU functions biologically as a homotrimer. The three N‐terminal uridyltransferase active sites are independently formed by each monomer; however, each of the three acetyltransferase active sites is comprised of residues from the beta‐helix domain of all three monomers. This site is formed by one face of the beta‐helix and a loop region of the first monomer, a different face of the second monomer beta‐helix, and the C‐terminal tail of the third monomer.Support or Funding InformationThis work was funded in part by NSF‐DUE 1725940 for the CREST Project and the Wabash College Haines Biochemistry fund.This abstract is from the Experimental Biology 2018 Meeting. There is no full text article associated with this abstract published in The FASEB Journal.