Crystal Structure of the Bacillus subtilis Phosphodiesterase PhoD Reveals an Iron and Calcium-containing Active Site

DOI: 10.1074/jbc.M114.604892
PMID: 25217636

Authors: Fernanda Rodriguez (Department of Biochemistry, University of Oxford) , James Lillington (Sir William Dunn School of Pathology, University of Oxford) , Steven Johnson (Sir William Dunn School of Pathology, University of Oxford) , Christiane R. Timmel (Inorganic Chemistry Laboratory, University of Oxford) , Susan Lea (Sir William Dunn School of Pathology, University of Oxford) , B. C. Berks (Department of Biochemistry, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Journal Of Biological Chemistry , VOL 289 (45) , PAGES 30889 - 30899

State: Published (Approved)
Published: November 2014
Diamond Proposal Number(s): 9306

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 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 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 Fe3+ and Ca2+ ions.

Subject Areas: Biology and Bio-materials, Chemistry


Instruments: I03-Macromolecular Crystallography

Other Facilities: ESRF ID23_1

Documents:
J. Biol. Chem.-2014-Rodriguez-30889-99.pdf

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