 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](rf5050fig2mag.jpg)
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Figure 2
Introduction of Cys84 yields a disulfide-crosslinked S100A6 dimer. (a) SDS–PAGE analysis of the S100A6 Y84C variant under reducing (Red) and nonreducing (Non-red) conditions. A band at double the size of that of the S100A6 monomer is visible under nonreducing conditions, indicating that the protein readily forms disulfide-crosslinked dimers in solution. (b) Crystallographic structure of the RAGE–S100A6 Y84C complex at 2.35 Å resolution. The biological assembly encompasses two molecules of RAGE bound to one S100A6 homodimer (2:2 complex). (c) Overlay of the refined atomic model with the final electron-density map (2Fo − Fc map, blue mesh, contoured at 1 r.m.s.d). (d) The RAGE–S100A6 Y84C complex (red) superimposes extremely well with the RAGE–S100A6 WT complex (blue). (e) Superimposition of the RAGE-bound S100A6 Y84C dimer (orange and teal) with the RAGE-bound S100A6 WT dimer (gray). Both adopt the same dimeric conformation. (f) Zoom on the C-terminal helices (H4) of both S100 protomers in the RAGE-bound S100A6 Y84C homodimer. The two protomers are covalently linked via an intermolecular disulfide bridge (Cys84–Cys84). The single simulated-annealing omit map calculated in phenix.refine after removing S100A6 residues Ile83–Asn85 in the model is displayed as blue mesh around this region (contoured at 1 r.m.s.d), allowing visualization of the clearly defined density for the S—S bond. |
![[Figure 2]](rf5050fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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