Publication Abstract from PubMed
The PhoD family of extracytoplasmic phosphodiesterases are amongst 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 Fe3+ ion. However, the PhoD active site diverges from that found in PAPs and uses two Ca2+ ions instead of the single extra Fe2+, Mn2+, or Zn2+ ion present in PAPs. The PhoD crystals contain a phosphate molecule that co-ordinates all three active site metal ions and which is proposed to represent a product complex. A C-terminal helix lies over the active site and controls access to the catalytic centre. The structure of PhoD defines a new phosphatase active site architecture based on Fe3+ and Ca2+ ions.
Crystal Structure of the Bacillus subtilis Phosphodiesterase PhoD Reveals an Iron and Calcium-Containing Active Site.,Rodriguez F, Lillington J, Johnson S, Timmel CR, Lea SM, Berks BC J Biol Chem. 2014 Sep 12. pii: jbc.M114.604892. PMID:25217636[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
