Figure 2.
Figure 2: RNase II–ssRNA interactions. Figure 2 :
RNase II|[ndash]|ssRNA interactions. Unfortunately we are
unable to provide accessible alternative text for this.
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a, Atomic interactions scheme between RNA (enclosed atoms in
black or in red for O2'-protein interactions) and protein
residues (coloured by domains as in Fig. 1a). Hb indicates
hydrogen bonds up to 3.2 Å, and vdW indicates van der
Waals interactions up to 3.6 Å. b, c, RNA docking
catalytic region (b) with residues 364–381 deleted for
clarity, and anchor region (c) involving canonical
oligonucleotide-binding motifs^16 L[23] of CSD2, and chain 3
and loop L[45] of S1. RNA (coloured as in Fig. 1) and protein
hydrogen-bonding side-chain residues shown in sticks (carbon in
yellow, nitrogen in cyan, oxygen in red), enzyme domains as
cartoons (coloured as in Fig. 1). Hydrogen bonds shown as dashed
green lines, Mg shown as green sphere with coordination in
dashed yellow lines. Nucleotides (Nt) 9–13 are clamped between
the aromatic side-chains of Tyr 253 and Phe 358 (with labels
highlighted in green), nucleotides 3 and 4 are between Phe 588
and Pro 104, and nucleotide 5 is nestled between His 103, Pro
104, Asp 102 and Arg 167.
3
and loop L[45] of S1. RNA (coloured as in Fig. 1) and protein
hydrogen-bonding side-chain residues shown in sticks (carbon in
yellow, nitrogen in cyan, oxygen in red), enzyme domains as
cartoons (coloured as in Fig. 1). Hydrogen bonds shown as dashed
green lines, Mg shown as green sphere with coordination in
dashed yellow lines. Nucleotides (Nt) 9–13 are clamped between
the aromatic side-chains of Tyr 253 and Phe 358 (with labels
highlighted in green), nucleotides 3 and 4 are between Phe 588
and Pro 104, and nucleotide 5 is nestled between His 103, Pro
104, Asp 102 and Arg 167.