5X9Q
Crystal structure of HldC from Burkholderia pseudomallei
Summary for 5X9Q
| Entry DOI | 10.2210/pdb5x9q/pdb |
| Descriptor | Putative cytidylyltransferase, 2-(N-MORPHOLINO)-ETHANESULFONIC ACID (3 entities in total) |
| Functional Keywords | d-glycero-beta-d-manno-heptose-1-phosphate adenylyltransferase, hldc, hlde2, heptose biosynthesis pathway, transferase |
| Biological source | Burkholderia pseudomallei (strain K96243) |
| Total number of polymer chains | 4 |
| Total formula weight | 75092.31 |
| Authors | Park, J.,Kim, H.,Kim, S.,Lee, D.,Shin, D.H. (deposition date: 2017-03-08, release date: 2017-12-27, Last modification date: 2024-03-27) |
| Primary citation | Park, J.,Kim, H.,Kim, S.,Lee, D.,Kim, M.S.,Shin, D.H. Crystal structure of D-glycero-Beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei. Proteins, 86:124-131, 2018 Cited by PubMed 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. PubMed: 28986923DOI: 10.1002/prot.25398 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
Download full validation report
