JBC's 'Paper of the Week' from the Berks' group

A recent paper from Professor Ben Berks' group has been selected as 'Paper of the Week' in the Journal of Biological Chemistry.

Cover of JBC's November 7 issue created by Ben Berks' lab. The illustration shows the structure of the PhoD enzyme from the soil bacterium Bacillus subtilis. The catalytic metal ions are presented as spheres, with iron shown in orange and calcium in purple

Cover of JBC's November 7 issue created by Ben Berks' lab. The illustration shows the structure of the PhoD enzyme from the soil bacterium Bacillus subtilis. (Click to enlarge)

The paper, which was determined as in the top two percent of manuscripts reviewed in significance and importance, describes the structure of a member of the bacterial alkaline phosphatase PhoD family and characterisation of its active site (1).

Following on from the Berks lab's recent paper showing that iron and calcium atoms combine to form a novel cofactor in the PhoX family of phosphatases (2), the JBC paper shows that the PhoD family uses the same metal ions but organised in a different way to catalyse phosphate cleavage.

This combination of metal ions has not previously been detected in other enzymes, so it is remarkable that the two families, which are structurally unrelated, share this in common.

With two out of the three major classes of bacterial extracellular phosphatases (PhoX and PhoD) now demonstrated to require iron for catalysis, it is highly likely that bacterial phosphorus nutrition is limited by the low concentrations of iron available in many environments.

Highlighting the paper in its Table of Contents, the journal profiles the joint first authors - Fernanda Rodriguez from Professor Berks' lab and James Lillington from the lab of collaborator Professor Susan Lea in the Dunn School of Pathology.

References

  1. Crystal Structure of the Bacillus subtilis Phosphodiesterase PhoD Reveals an Iron and Calcium-Containing Active Site. Rodriquez, F, Lillington, J, Johnson, S, Timmel, CG, Lea, SM and Berks, B. Journal of Biological Chemistry (2014) 289:30889-30899 and commentary: http://www.jbc.org/content/289/45/30900.full.html
  2. http://www.bioch.ox.ac.uk/aspsite/index.asp?pageid=1176

 

 

 

 

 





Page Last Updated: 07/11/2014 by Webmaster
© 2014 Department of Biochemistry