6k63

The crystal structure of cytidine deaminase from Klebsiella pneumoniae

spinqualitylabelsall models 6k63, resolution 2.07Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6k63 is a 4 chain structure with sequence from Klebsiella pneumoniae subsp. pneumoniae MGH 78578. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.073Å Ligands: DIO, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function CDD_KLEP7 This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.[HAMAP-Rule:MF_01558] Publication Abstract from PubMed The emergence of drug-resistant strains of Klebsiella pneumoniae, has exacerbated the treatment and control of the disease caused by this bacterium. Cytidine deaminases (CDA) are zinc-dependent enzymes involved in the pyrimidine salvage pathway and catalyze the formation of uridine and deoxyuridine from cytidine and deoxycytidine, respectively. To illustrate the structural basis of CDA for a deeper knowledge of the molecular mechanisms underlying the salvage pathway, we reported here the biochemical and structural analysis of CDA from pathogenic K. pneumonia. KpCDA showed deaminase activity against cytidine as well as its analog cytarabine. The deaminase activity of KpCDA on cytarabine was 1.8 times higher than that on cytidine. KpCDA is composed of an N-terminal catalytic domain and a C-terminal noncatalytic domain. Zinc, which is involved in the activity of the catalytic domain, is coordinated by His102, Cys129, and Cys132, and two 1,4-dioxane molecules were present at the active sites. KpCDA exists as a dimer and shows distinct dimeric interface compared with other CDAs. Our results provide the structural features of KpCDA, and KpCDA might be a potential antibacterial target for the disease caused by K. pneumoniae. Biochemical and structural analysis of the Klebsiella pneumoniae cytidine deaminase CDA.,Liu W, Shang F, Chen Y, Lan J, Wang L, Chen J, Gao P, Ha NC, Quan C, Nam KH, Xu Y Biochem Biophys Res Commun. 2019 Nov 5;519(2):280-286. doi:, 10.1016/j.bbrc.2019.08.167. Epub 2019 Sep 5. PMID:31495495 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Deaminase 3D structures

Proteopedia Page Contributors and Editors (what is this?)

OCA