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- W2763674517 abstract "The crystal structure of HldC from B. pseudomallei (BpHldC), the fourth enzyme of the heptose biosynthesis pathway, has been determined. BpHldC 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 BpHldC 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 BpHldC indicate that the core catalytic mechanism of BpHldC 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." @default.
- W2763674517 created "2017-10-20" @default.
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- W2763674517 date "2017-10-31" @default.
- W2763674517 modified "2023-10-01" @default.
- W2763674517 title "Crystal structure of D-glycero-Β-D-manno-heptose-1-phosphate adenylyltransferase fromBurkholderia pseudomallei" @default.
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- W2763674517 doi "https://doi.org/10.1002/prot.25398" @default.
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