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Figure 2
Interfaces among the components of the DA2E subcomplex. (a) Overall view of the DA2E structure showing the interfaces between DRS and AIMP2GST and between AIMP2GST and EPRSGST. (b) Close-up view of interactions between DRS (green) and AIMP2GST (orange). Hydrogen bonds and salt bridges between DRS and AIMP2GST are indicated by purple dashed lines. (c) Stereoscopic representation showing the effect of DRS incorporation on the AIMP2GST–EPRSGST interface. The AIMP2GST structure from A2E (PDB entry 5a34; white) was superposed onto the DA2E structure (orange) to show conformational change in the β4–β5 loop. The β4–β5 loop region of AIMP2GST from the A2E subcomplex (red circle) collides with helix α9 of DRS shown in transparent cartoon representation (green). The first and the last residues of the β4–β5 loop (Lys198 and Pro206) are marked with cyan and red stars, respectively. (d) Size-exclusion chromatography analyses of Ser156 mutants on DA2 complex formation. (e) R.m.s.d. analysis of AIMP2GST structures in DA2E and the heterodimeric complex, showing remarkably large differences in the structures at the β4–β5 loop (Lys198–Pro206), highlighted in a yellow box.

IUCrJ
Volume 6| Part 5| September 2019| Pages 958-967
ISSN: 2052-2525