journal menu
![[Figure 1]](mn5067fig1mag.jpg)
|
|
Figure 1
Sequence and structure of NucA. (a) Sequence of full-length GBS_NucA. The putative transmembrane secretion signal is shown in pink. Protease cleavage is thought to occur between residues Ala38 and Asp39 (gray). This region is not included in the crystallization construct (starting at Ser42, black asterisk). The DXGH motif is colored in yellow. Mutations hypothesized to interfere with DNA binding are marked in purple and all other mutations used in this study are marked in cyan. Residues along the substrate-binding loop are shown in red. `Finger loop' residues are boxed in orange. Secondary-structural elements are shown above the sequence, with α-helices (blue) labeled alphabetically and β-strands (green) numbered. (b) Superposition of GBS_NucA apoprotein (gray) and Mg2+-bound GBS_NucA (α-helices in blue, β-strands in green and coils in yellow) as viewed from the `front' face of the enzyme. α-Helices and β-strands are colored and numbered as described in (a). The `finger loop' insertion in α-helix C is shown in orange. Disordered residues of the substrate-binding loop in the apoprotein are numbered in black and the ordered substrate-binding loop from the Mg2+-bound GBS_NucA is shown in red. (c) Superposition of GBS_NucA in space group P1 (gray) and P63 (α-helices in blue, β-strands in green and coils in yellow) as viewed from the `back' face, a 180° vertical rotation from (b). Structural figures were created using PyMOL (https://www.pymol.org), using molecule A from each space group. |
![[Figure 1]](mn5067fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
Open 
access
access
