Fig. 2: Overview of the obtained crystallographic NMT complexes. | Nature Communications

Fig. 2: Overview of the obtained crystallographic NMT complexes.

From: High-resolution snapshots of human N-myristoyltransferase in action illuminate a mechanism promoting N-terminal Lys and Gly myristoylation

Fig. 2

Crystal structures of HsNMT1 in complex with substrates, TI and products obtained with different peptides X, Y and Z. The HsNMT1 main chain is displayed as a green ribbon. Substrates, TI and products are displayed as sticks and are indicated with black arrows. a Crystal structure of HsNMT1 in complex with MyrCoA and peptide X (green). b Crystal structure of HsNMT1 in complex with TI-Y, in which peptide Y and CoA are coloured in cyan. c Crystal structure of HsNMT1 in complex with MyrY and CoA (orange) products. d Crystal structure of HsNMT1 in complex with MyrZ product coloured in pink. e–h Detail of the “fofc omit” sigmaA-weighted electron density maps (mFobs – DFcalc, PHIcalc), shown in grey, for substrates, TI and products (in sticks coloured as in a–d). The omit electron density maps were calculated after a round of refinement in which the occupancy of substrates, TI and products was set to zero. The e/Å3 value of each “2fofc omit” sigmaA-weighted electron density map (2mFobs – DFcalc, PHIcalc) at 0.92–1 rmsd level (0.25, 0.33, 0.33 and 0.30 e/Å3 for X, TI-Y, Myr-Y and Myr-Z, respectively) was used as reference to set the contoured value of fofc omit electron density maps shown. Peptide, Myr, MyrCoA and CoA moieties are indicated with black arrows.

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