8yt5

SP1746 treated with EDTA, in complex with ADP

spinqualitylabelsall models 8yt5, resolution 1.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 8yt5 is a 1 chain structure with sequence from Streptococcus pneumoniae TIGR4. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A0H2URF8_STRPN Publication Abstract from PubMed In this report, we structurally and biochemically characterized the unknown gene product SP1746 from Streptococcus pneumoniae serotype 4. Various crystal structures of SP1746 in the apo form and in complex with different nucleotides were determined. SP1746 is a globular protein, which belongs to the histidine-aspartate (HD) domain superfamily with two Fe(3+) ions in the active site that are coordinated by key active site residues and water molecules. All nucleotides bind in a similar orientation in the active site with their phosphate groups anchored to the diiron cluster. Biochemically, SP1746 hydrolyzes different nucleotide substrates. SP1746 most effectively hydrolyzes diadenosine tetraphosphate (Ap4A) to two ADPs. Based on the aforementioned data, we annotated SP1746 as an Ap4A hydrolase, belonging to the YqeK family. Our in vitro data indicate a potential role for SP1746 in regulating Ap4A homeostasis, which requires validation with in vivo experiments in bacteria in the future. Structural and biochemical characterization of a nucleotide hydrolase from Streptococcus pneumonia.,Jin Y, Ke J, Zheng P, Zhang H, Zhu Z, Niu L Structure. 2024 Aug 8;32(8):1197-1207.e4. doi: 10.1016/j.str.2024.04.009. Epub , 2024 May 2. PMID:38701795 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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