 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 3]](ub5080fig3mag.jpg)
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Figure 3
Domain motions in TpCS(H6). Each panel shows the open TpCSH6 structure superimposed on a closed TpCS structure in pairwise DynDom analyses. The static portion, mainly the large domains that form the majority of the dimer interface, is shown as a surface rendering. The mobile domain extends from the surface and is shown in cartoon rendering, with the TpCSH6 mobile region colored red and the closed structure colored grey. Hinging residues in each TpCSH6 domain are colored yellow. Residues involved in each pairwise comparison are shown in Supplementary Fig. S7. The rotation axis is shown as a black bar; closure results in clockwise rotations about this axis. (a) Comparison with the TpCS–OAA complex (PDB entry 2ifc subunit A) shows 52% closure and a 8.9° rotation (translation of 0.1 Å). Mobile domain: 99 residues, r.m.s.d. 0.41 Å. Static domain: 277 residues, r.m.s.d. 0.52 Å. (b) Comparison with the TpCS–OAA–CMCoA complex (PDB entry 2r26 subunit A) shows 86% closure and a 10.6° rotation (translation of 0.4 Å). Mobile domain: 115 residues, r.m.s.d. 0.68 Å. Static domain: 258 residues, r.m.s.d. 0.69 Å. CMCoA is a tight-binding analogue of the deprotonated AcCoA formed during the condensation reaction. (c) Comparison with the TpCS–CitMX complex (PDB entry 2r9e subunit B) shows 82% closure and a 10.3° rotation (translation 0.4 Å). Mobile domain: 123 residues, r.m.s.d. 0.83 Å. Static domain: 252 residues, r.m.s.d. 0.7 Å. CitMX is formed from AcMX and OAA, presumably within the crystal. |
![[Figure 3]](ub5080fig3.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
