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In the biofilm regulation pathway of Pseudomonas fluorescens and similar bacteria, high phosphate levels lead to the creation of messenger molecule cyclic-di-guanosin monophosphate (CDGMP). cdGMP activates key regulatory protein LapD through its cytoplasmic domains. LapD then, through its periplasmic domains, binds to enzyme LapG, which keeps LapG from breaking down the molecule responsible for the biofilm assembly, the elastin LapA.

A few years ago the Sondermann group used MacCHESS facilities to solve several molecular structures of cytoplasmic domains of the LapD regulatory protein from Pseudomonas fluorescens, alone and in complex with signaling molecule cdGMP. (Navarro, et al., 2011 DOI 10.1371/JOURNAL.PBIO.1000588)

They also used MacCHESS facilites to solve several structures of the LapG enzyme. (Chatterjee, et al. 2012, 10.1128/JB.00640-12)

For the most recent publication, the Sondermann group returned to MacCHESS to solve structures of the periplasmic domain of protein CdgS9 from Legionella pneumophila (an analog of Pseudomonas LapD) both alone and in complex with LapG. These latest structures reveal much detail about the key binding interface between these proteins.

Read the Cornell Chronicle article here:



Submitted by: David Schuller, CHESS, Cornell University