Fig. 6: Interaction of K220 in the RT active site.
From: Structural basis of deoxynucleotide addition by HIV-1 RT during reverse transcription
Structural changes of K220 during HIV-1 RT reaction. a The arrival of dATP to the active site forces a repositioning (Black arrow) in K220 to avoid clashes (red, dATP-free state, map in red mesh with B-factor −40 Å2 and contoured at 6.5σ; yellow, state R-1, map in yellow mesh with B-factor −60 Å2 and contoured at 12σ). b K220 directly interacts with the phosphate tail of dATP-i prior to nucleotide addition (gray, state T8sec; map in gray mesh with B-factor −60 Å2 and contoured at 8σ). c Following translocation (green, state P6min, map in green mesh with B-factor −60 Å2 and contoured at 8σ), a second conformation for K220 is detected (marked with *). d Overlay of all stages showing the movement of K220 during the dATP addition cycle (including state R-2, in blue). Coordination distances (in Å) are indicated next to dashed lines. e Transient kinetic analysis of nucleotidyl transfer by wild-type (WT), K220L, and K220M HIV-1 RT. Data represent mean ± SD (n = 3). f Replication capacity of wild-type, K220L and K220M HIV-1 in TZM-bl cells. Source data are provided as a Source Data file.
