5x9q | pdb_00005x9q

Crystal structure of HldC from Burkholderia pseudomallei

spinqualitylabelsall models 5x9q, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5x9q is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MES Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [Q63XZ4_BURPS] Catalyzes the ADP transfer from ATP to D-glycero-beta-D-manno-heptose 1-phosphate, yielding ADP-D-glycero-beta-D-manno-heptose.[SAAS:SAAS00558028] Publication Abstract from PubMed 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-beta-d-manno-heptose-1-phosphate into ADP-d-glycero-beta-d-manno-heptose and pyrophosphate. The crystal structure of BpHldC belongs to the nucleotidyltransferase alpha/beta phosphodiesterase superfamily sharing a common Rossmann-like alpha/beta 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. Crystal structure of D-glycero-Beta-D-manno-heptose-1-phosphate adenylyltransferase from Burkholderia pseudomallei.,Park J, Kim H, Kim S, Lee D, Kim MS, Shin DH Proteins. 2018 Jan;86(1):124-131. doi: 10.1002/prot.25398. Epub 2017 Oct 31. PMID:28986923 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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