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![[Figure 2]](ud5029fig2mag.jpg)
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Figure 2
CryoEM structure of SoBDH2. (a) Tetrameric assembly of SoBDH2. Density at a contour level of 1.1 is shown for each of the four protomers in different shades of green after sharpening with Phenix. The locations of very well defined water molecules are shown in red. (b) The same color-coding as in (a), but rotated by 90°. (c) Grouped B factor mapped onto the density. The color gradient is from blue to red corresponding to increasing B factors. Regions with high B factors are highlighted with gray ellipses and are labeled according to the assigned secondary structure. (d) SoBDH2 structure in cartoon representation. The same view and color-coding as in (a) is used. (e) Structure-based sequence alignment of SrBDH1 (GenBank ID MT857224) and SoBDH2 (GenBank ID MT525099) as obtained by cryoEM. Secondary-structure elements are drawn above the alignment for SrBDH1 and below the alignment for SoBDH2, with α-helices depicted as cylinders and β-strands as arrows. Gray inclined lines indicate sections of the structures which could not be modeled since they were not resolved in the reconstruction. Orange triangles indicate the catalytic motif. Amino acids lining the putative active site of SrBDH1, based on its crystal structure (PDB entry 6zyz) with bound NAD+, are indicated by blue triangles and by a dark blue circle if derived from the C-terminal portion of another SrBDH1 monomer within the tetramer. The dark green circle marks a residue derived from another protomer of SoBDH2 that completes the active site. Gray-shaded amino acids are identical. The TGXXX(AG)XG NAD+-binding motif, between βA and αB, is indicated with a magenta rectangle. |
![[Figure 2]](ud5029fig2.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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