6jyy | pdb_00006jyy

Crystal structure of the 5-(Hydroxyethyl)-methylthiazole Kinase ThiM from Klebsiella pneumonia

spinqualitylabelsall models 6jyy, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6jyy is a 3 chain structure with sequence from "bacillus_pneumoniae"_(schroeter_1886)_flugge_1886 "bacillus pneumoniae" (schroeter 1886) flugge 1886. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: thiM, BN49_3768 ("Bacillus pneumoniae" (Schroeter 1886) Flugge 1886) Activity: Transferase, with EC number 2.7.1.50 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [W9BB97_KLEPN] Catalyzes the phosphorylation of the hydroxyl group of 4-methyl-5-beta-hydroxyethylthiazole (THZ).[HAMAP-Rule:MF_00228][SAAS:SAAS00158945] Publication Abstract from PubMed Thiamin pyrophosphate (TPP) is an essential co-factor in amino acid and carbohydrate metabolic pathways. The TPP-related vitamin B1 biosynthetic pathway is found in most bacterial, plant and lower eukaryotic processes; however, it is not present in humans. In bacterial thiamin synthesis and salvage pathways, the 5-(hydroxyethyl)-methylthiazole kinase (ThiM) is essential in the pathway forming TPP. Thus, ThiM is considered to be an attractive antibacterial drug target. Here, we determined the crystal structures of ThiM from pathogenic Klebsiella pneumoniae (KpThiM) and KpThiM in complex with its substrate 5-(hydroxyethyl)-4-methylthiazole (TZE). KpThiM, consisting of an alpha-beta-alpha domain, shows a pseudosymmetric trimeric formation. TZE molecules are located in the interface between the KpThiM subunits in the trimer and interact with Met49 and Cys200. Superimposition of the apo and TZE-complexed structures of KpThiM show that the side chains of the amino acids interacting with TZE and Mg(2+) have a rigid configuration. Comparison of the ThiM structures shows that KpThiM could, in terms of sequence and configuration, be different from other ThiM proteins, which possess different amino acids that recognize TZE and Mg(2+). The structures will provide new insight into the ThiM subfamily proteins for antibacterial drug development. Structural insight of the 5-(Hydroxyethyl)-methylthiazole kinase ThiM involving vitamin B1 biosynthetic pathway from the Klebsiella pneumoniae.,Chen Y, Wang L, Shang F, Liu W, Lan J, Chen J, Ha NC, Quan C, Nam KH, Xu Y Biochem Biophys Res Commun. 2019 Oct 20;518(3):513-518. doi:, 10.1016/j.bbrc.2019.08.086. Epub 2019 Aug 19. PMID:31439375 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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