Crystal structure of D‐ glycero glycero ‐ Β Β ‐D‐ manno manno ‐heptose‐1‐phosphate adenylyltransferase from Burkholderia pseudomallei Burkholderia pseudomallei

摘要

Abstract The crystal structure of HldC from B. pseudomallei ( Bp HldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. Bp HldC converts ATP and d ‐ glycero ‐β‐ d ‐ manno ‐heptose‐1‐phosphate into ADP‐ d ‐ glycero ‐β ‐d ‐ manno ‐heptose and pyrophosphate. The crystal structure of Bp HldC belongs to the nucleotidyltransferase α/β phosphodiesterase superfamily sharing a common Rossmann‐like α/β fold with a conserved T/HXGH sequence motif. The invariant catalytic key residues of Bp HldC indicate that the core catalytic mechanism of Bp HldC may be similar to that of other closest homologues. Intriguingly, a reorientation of the C‐terminal helix seems to guide open and close states of the active site for the catalytic reaction.