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A P P L I C A T I O N N O T E
PROTEIN 2: PGLB BACKGROUND
PglB from Neisseria Gonorrhoeae contains
a membrane-embedded phosphoglycosyl
transferase domain fused to a soluble
acetyltransferase (AT) domain and is involved in
the production of extracellular polysaccharides.
This bifunctional enzyme acetylates a UDP-
sugar substrate, and then transfers the resulting
acetylated phosphosugar onto Und-P. Structural
studies on related ATs support that this domain
mediates trimerization of the dual-function
membrane protein. While there are structures of
homologs for both subdomains, the structure of
the full-length protein is of considerable interest
for understanding the coordination of two
sequential steps.
PROTEIN 3: PGLC BACKGROUND
PglC from Helicobacter Pullorum is a small
membrane protein with an unusual topology,
as it contains a single re-entrant membrane
helix that enters and exits the bilayer on the
same face. Like the above proteins, Hp PglC
functions in the early stages of glycoconjugate
biosynthesis, transferring the phosphosugar
moeity from UDP-diNAcBac onto Und-P. While
the small size of this protein (~20 kDa) precludes
cryo-EM structure determination on its own,
addition of mass fiduciaries in the form of fAbs,
legobodies, or pro-macrobodies may represent
a path to visualize the structure of this small
protein in a native-like bilayer.
DIBMA
Class of copolymers included in the Cube Synthetic Nanodisc screening Kit MAXI
ULTRASOLUTE
TM
AMPHIPOL
