25xa

Crystal structure of bacterial DUSP from Candidatus Chlorohelix allophototropha

spinqualitylabelsall models 25xa, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 25xa is a 2 chain structure with sequence from Chloroflexia. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.4Å Ligands: CL, SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A8T7M2Z3_9CHLR Publication Abstract from PubMed Dual specificity phosphatases (DUSPs) are a subfamily of protein tyrosine phosphatases that regulate diverse cellular processes through dephosphorylation of phosphorylated substrates. DUSPs are commonly found in eukaryotes, bacteria, archaea, and viruses. However, structural and biochemical characterization of bacterial DUSP remains limited, as only one bacterial DUSP has been identified thus far. In this study, we investigated a novel putative bacterial DUSP from Candidatus Chlorohelix allophototropha, referred to as CCaDUSP. The crystal structure of CCaDUSP showed the presence of a well-conserved catalytic motif with a characteristic phosphate-binding loop. Biochemical analyses further confirmed that CCaDUSP exhibits phosphatase activity and contains dual general acid/base residues, both of which contribute to its enzymatic activity. These findings not only represent the first characterization of a novel bacterial DUSP with dual general acid/base residues but also provide a foundation for understanding the diversity of DUSP proteins in bacteria. Structural and biochemical analyses of a novel bacterial dual specificity phosphatase from Candidatus Chlorohelix allophototropha.,Jung S, Park SH, Choi JS, Shin HC, Kim SJ, Ku B J Microbiol. 2026 Jul;64(7):e2604025. doi: 10.71150/jm.2604025. Epub 2026 Jul 16. PMID:42457432 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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