ArticleThe Journal of biological chemistry2014
Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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35 citing papers in PubMed, 84 citations in OpenAlex.
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- The Fe and Zn cofactor dilemma.Biochimica et biophysica acta. Proteins and proteomics · 2023Review
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- Achieving Selectivity for Phosphate over Pyrophosphate in Ethanol with Iron(III)-Based Fluorescent Probes.JACS Au · 2022Article
- Phosphorus Limitation Enhances Diazotroph Zinc Quotas.Frontiers in microbiology · 2022Article
- Enzyme promiscuity in natural environments: alkaline phosphatase in the ocean.The ISME journal · 2021Article
- The DNA transporter ComEC has metal-dependent nuclease activity that is important for natural transformation.Molecular microbiology · 2021Article
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- Torpedo californica acetylcholinesterase is stabilized by binding of a divalent metal ion to a novel and versatile 4D motif.Protein science : a publication of the Protein Society · 2021Article
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6 authors at 1 institution in 1 country.
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Abstract
The PhoD family of extra-cytoplasmic phosphodiesterases are among the most commonly occurring bacterial phosphatases. The exemplars for this family are the PhoD protein of Bacillus subtilis and the phospholipase D of Streptomyces chromofuscus. We present the crystal structure of B. subtilis PhoD. PhoD is most closely related to purple acid phosphatases (PAPs) with both types of enzyme containing a tyrosinate-ligated Fe(3+) ion. However, the PhoD active site diverges from that found in PAPs and uses two Ca(2+) ions instead of the single extra Fe(2+), Mn(2+), or Zn(2+) ion present in PAPs. The PhoD crystals contain a phosphate molecule that coordinates all three active site metal ions and that is proposed to represent a product complex. A C-terminal helix lies over the active site and controls access to the catalytic center. The structure of PhoD defines a new phosphatase active site architecture based on Fe(3+) and Ca(2+) ions.
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