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![[Figure 3]](mn5067fig3mag.jpg)
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Figure 3
Structural homology with related sequence/structure-nonspecific nucleases. (a) Sequence alignment of the ββα-Me finger motif from structurally similar nucleases, as calculated using the DALI server (Holm & Rosenström, 2010  ). Nucleases included in this list include EndA from S. pneumoniae, Spd1 from S. pyogenes encoded by the SF370.1 prophage, SM nuclease from Serratia marcescens and NucA from Anabaena sp. The positions of the β-strands are marked by green arrows and the α-helix by a blue rectangle (corresponding to β-strands 7–8 and α-helix C in GBS_NucA). Conserved residues are boxed in black. Key residues for catalytic function are shown in red. The `finger loop' from Streptococcus sp. nucleases is boxed in orange. Residue numbers are indicated to the right of the alignment, and the Z-scores and structure-based sequence identities (as calculated by the DALI server) are listed on the far right. Sequence interruptions of the VVN nuclease sequence are shown as repeated dots, with the residue numbers below. (b, c, d) Structural superposition of GBS_NucA (H148A) (blue) and EndA (H160A) (PDB entry 3owv; Moon et al., 2011; orange), emphasizing the `front' (b), `back' (c) and `side' (d) faces of the enzymes. (e, f, g) Structural superposition of GBS_NucA (H148A) (blue) and Spd1 (PDB entry 2xgr (Korczynska et al., 2012; green), emphasizing the `front' (e), `back' (f) and `side' (g) faces of the enzymes. Dashed circles highlight regions of structural dissimilarity. |
![[Figure 3]](mn5067fig3.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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