8JK8
SP1746 in complex with UDP
Summary for 8JK8
| Entry DOI | 10.2210/pdb8jk8/pdb |
| Descriptor | bis(5'-nucleosyl)-tetraphosphatase (symmetrical), FE (III) ION, URIDINE-5'-DIPHOSPHATE, ... (7 entities in total) |
| Functional Keywords | enzyme, hydrolase, hd domain superfamily protein, phosphohydrolase, unknown gene product, sp1746 |
| Biological source | Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4) |
| Total number of polymer chains | 1 |
| Total formula weight | 26009.44 |
| Authors | |
| Primary citation | Jin, Y.,Ke, J.,Zheng, P.,Zhang, H.,Zhu, Z.,Niu, L. Structural and biochemical characterization of a nucleotide hydrolase from Streptococcus pneumonia. Structure, 32:1197-1207.e4, 2024 Cited by PubMed Abstract: 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 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. PubMed: 38701795DOI: 10.1016/j.str.2024.04.009 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.95 Å) |
Structure validation
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