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. Author manuscript; available in PMC: 2015 Jul 1.
Published in final edited form as: Nat Chem Biol. 2014 Nov 10;11(1):26–32. doi: 10.1038/nchembio.1687

Figure 4. Effect of the structural rearrangement on the enzymatic actiivty.

Figure 4

Cut-away views of the protein surface at the active sites of HRASLS3/LRAT (a) and native HRASLS3 (b). Protein structures were aligned to ensure identical orientations. The NMR structure of HRASLS3 (PDB accession – 2KYT) was used for this figure. (c) Rates of phospholipid hydrolysis as a function of phospholipid substrate concentration for HRASLS3 (●) and its chimeric counterpart (○). (d) Stability of protein thioester adducts. The modified form of HRASLS3 steadily declines in the absence of phospholipid substrate, whereas the HRASLS3/LRAT thioester form remains intact for the duration of this experiment. Data represent mean values from three independent experiments performed in duplicates. Error bars, s.d.