25XA

Crystal structure of bacterial DUSP from Candidatus Chlorohelix allophototropha

Summary for 25XA

• Entry DOI: 10.2210/pdb25xa/pdb
• Descriptor: Dual specificity protein phosphatase family protein, SULFATE ION, CHLORIDE ION, ... (4 entities in total)
• Functional Keywords: protein tyrosine phosphatase; ptp; dual specificity phosphatase; dusp; candidatus chlorohelix allophototropha; ccadusp, hydrolase
• Biological source: Candidatus Chlorohelix allophototropha
• Total number of polymer chains: 2
• Total formula weight: 37206.05

Authors

Jung, S.,Ku, B. (deposition date: 2026-04-21, release date: 2026-08-12)

Primary citation

Jung, S.,Park, S.H.,Choi, J.S.,Shin, H.C.,Kim, S.J.,Ku, B.
Structural and biochemical analyses of a novel bacterial dual specificity phosphatase from Candidatus Chlorohelix allophototropha.
J.Microbiol, 64:e2604025-e2604025, 2026

PubMed Abstract: 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.

PubMed: 42457432
DOI: 10.71150/jm.2604025

Experimental method

X-RAY DIFFRACTION (2.4 Å)