 | Acta Crystallographica Section D Acta Crystallographica Section D BIOLOGICAL CRYSTALLOGRAPHY |
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![[Figure 1]](ba0048fig1mag.jpg)
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Figure 1
Structure of the GroEL subunit in relation to the oligomer. One GroEL subunit has been outlined in a 15 Å representation of the 14-mer (left) with an expanded view of the subunit from X-ray crystallography shown on the right. Three domains are shown colour coded: apical (purple), intermediate (orange) and equatorial (green). They are separated by two hinge regions, which are rich in conserved glycines (Fenton et al., 1994  ). The domains are colour coded as defined for the docking trial. Regions of grey between them correspond to short loops between the domains that were not defined as part of any domain. The equatorial domain contains the ATP-binding site (shown here containing the non-hydrolysable ATP analogue ATPγS drawn in space-filling representation) and forms inter- and intra-ring contacts. The intermediate domain joins the equatorial and apical domains and contains residues involved in ATP hydrolysis. The apical domain contains residues required for substrate–protein and GroES binding, shown in space-filling representation in yellow and blue, respectively. The equatorial domain contains the amino (N) and carboxy (C) termini of the protein chain. The diameter of the oligomer is ∼140 Å. AVS was used to generate the isosurface of a 15 Å map calculated from the coordinates of the GroEL 14-mer (PDB accession number 1oel; Braig et al., 1995). The subunit was drawn with RASMOL, using a subunit extracted from the coordinates of the GroEL–ATPγS complex (PDB accession number 1der; Boisvert et al., 1996). Adapted from Roseman et al. (1996). |
![[Figure 1]](ba0048fig1.jpg)
| BIOLOGICAL CRYSTALLOGRAPHY |
ISSN: 1399-0047
