4s1m

Crystal Structure of Pyridoxal Kinase from Entamoeba histolyticaCrystal Structure of Pyridoxal Kinase from Entamoeba histolytica

Structural highlights 4s1m is a 2 chain structure with sequence from Entamoeba histolytica. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.64Å Ligands: , Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function C4LVZ4_ENTH1 Publication Abstract from PubMed Pyridoxal 5'-phosphate (PLP) is the active form of vitamin B6 and a cofactor for more than 140 enzymes. This coenzyme plays a pivotal role in catalysis of various enzymatic reactions that are critical for the survival of organisms. Entamoeba histolytica depends on the uptake of pyridoxal (PL), a B6 vitamer from the external environment which is then phosphorylated by pyridoxal kinase (EhPLK) to form PLP via the salvage pathway. E. histolytica cannot synthesise vitamin B6de-novo, and also lacks pyridoxine 5'-phosphate oxidase, a salvage pathway enzyme required to produce PLP from pyridoxine phosphate (PNP) and pyridoxamine phosphate (PMP). Analysing the importance of PLK in E. histolytica, we have determined the high-resolution crystal structures of the dimeric pyridoxal kinase in apo, ADP-bound, and PLP-bound states. These structures provided a snapshot of the transition state and help in understanding the reaction mechanism in greater detail. The EhPLK structure significantly differed from the human homologue at its PLP binding site, and the phylogenetic study also revealed its divergence from human PLK. Further, gene regulation of EhPLK using sense and antisense RNA showed that any change in optimal level is harmful to the pathogen. Biochemical and in vivo studies unveiled EhPLK to be essential for this pathogen, while the molecular differences with human PLK structure can be exploited for the structure-guided design of EhPLK inhibitors. Characterization and functional insights into the Entamoeba histolytica pyridoxal kinase, an enzyme essential for its survival.,Tarique KF, Devi S, Tomar P, Ali MF, Rehman SAA, Gourinath S J Struct Biol. 2020 Dec 1;212(3):107645. doi: 10.1016/j.jsb.2020.107645. Epub, 2020 Oct 9. PMID:33045383 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Pyridoxal kinase

spinqualitylabelsall models 4s1m, resolution 1.64Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image