Figure 4: DIPPS active site along with HMM logo and functional assays. | Nature Communications

Figure 4: DIPPS active site along with HMM logo and functional assays.

From: X-ray structure of a CDP-alcohol phosphatidyltransferase membrane enzyme and insights into its catalytic mechanism

Figure 4

(a) Zoomed view of the electron density map around the conserved aspartate residues. The maps were calculated before insertion of the magnesium ion in the model. The 2Fo–Fc density is shown in black and contoured at 1.5σ, the Fo–Fc density is green and contoured at 3σ; electron density around Asp357 is not very well defined. (b) HMM logo50 around the consensus sequence of CDP-alcohol phosphotransferase family based on the alignment of 124 representative Pfam protein families as seeds51. The most conserved residues are located at the intracellular ends of TM2 and TM3. (c) Diagram of DIPPS activity as assessed in 30 min reactions to study the effect of point mutations; values are expressed as % relative to the wild type enzyme in the presence of 10 mM Mg2+. Values are averages of duplicate experiments derived from independent growths.

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