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![[Figure 1]](ni5026fig1mag.jpg)
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Figure 1
Crystal structures of hBRR2T1 and the binding site of sulfaguanidine. (a) Domain scheme of hBRR2T1. hBRR2T1 comprises tandem helicase cassettes (NC, N-terminal helicase cassette; CC, C-terminal helicase cassette), each containing dual RecA-like domains (RecA1 and RecA2), a winged-helix (WH) domain, a helical bundle (HB) domain, a helix–loop–helix (HLH) domain and an immunoglobulin-like (IG) domain. The HB, HLH and IG domains form Sec63 homolog units. (b) Crystal structure of isolated hBRR2T1 in complex with sulfaguanidine (boxed). Unless mentioned otherwise, in this and the following figures or figure panels, hBRR2 domains are coloured according to the scheme in (a). (c) Sulfaguanidine binding pocket in isolated hBRR2T1. Residues of hBRR2T1 involved in the binding of sulfaguanidine are shown as sticks and are coloured by atom type. Unless mentioned otherwise, in this and the following figures or figure panels, protein C atoms are coloured as the respective protein region, compound C atoms in light grey, N atoms in blue, O atoms in red and S atoms in yellow; violet dashed lines represent van der Waals interactions or π-stacking interactions and yellow dashed lines represent hydrogen bonds. (d) Crystal structure of the hBRR2T1–hJab1ΔC complex (PDB entry 6s8q). Unless mentioned otherwise, in this and the following figures or figure panels, hJab1ΔC is shown in gold. (e) Selected interatomic distances between residues of the NC and the CC in the hBRR2T1–sulfaguanidine complex structure (left panel) and in the hBRR2T1–hJab1ΔC structure (right panel) are shown as pink dashed lines. Bound sulfaguanidine was omitted from the left panel. |
![[Figure 1]](ni5026fig1.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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