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.
| Original language | English |
|---|---|
| Pages (from-to) | 124-131 |
| Number of pages | 8 |
| Journal | Proteins: Structure, Function and Bioinformatics |
| Volume | 86 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2018 |
Bibliographical note
Funding Information:We are grateful to Dr. Sarinna Tumapa at Mahidol University and Dr. Sharon Peacock at University of Cambridge for their kindness in providing us with B. pseudomallei genomic DNA and the staff at Pohang Light Source for their assistance with synchrotron data collection. This research was supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (2015R1D1A1A01058942). J. Park was supported by Brain Korea 21 (BK21) Project.
Publisher Copyright:
© 2017 Wiley Periodicals, Inc.
Keywords
- HldC
- heptose biosynthesis pathway
- lipopolysaccharide
- melioidosis
- nucleotidyltransferase