Crystal structure of the Bacillus subtilis phosphodiesterase PhoD reveals an iron and calcium-containing active site

Fernanda Rodriguez, James Lillington, Steven Johnson, Christiane R. Timmel, Susan M. Lea, Ben C. Berks

Research output: Contribution to journalArticleResearchpeer-review

20 Citations (Scopus)

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+ orZn2+ 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.

Original languageEnglish
Pages (from-to)30889-30899
Number of pages11
JournalThe Journal of Biological Chemistry
Volume289
Issue number45
DOIs
Publication statusPublished - 7 Nov 2014
Externally publishedYes

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