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![[Figure 8]](ai5014fig8mag.jpg)
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Figure 8
Model-building and structural details of the GroEL–γATP complex. (a) Schematic workflow of the model-building and refinement process. The starting model for structural refinement was PDB entry 9c0c (apo GroEL). Initially, the model was fitted into the final map using UCSF ChimeraX, followed by manual adjustments in Coot. Iterative refinement cycles were performed in Phenix (phenix.real_space_refine) and structure validation was carried out using MolProbity. The resulting models have favorable stereochemical parameters, including minimal deviation from ideal bond lengths and angles, and a low number of macromolecular backbone outliers. (b) A side view of the multimeric GroEL complex is shown on the left, with each of the 14 subunits colored differently. The middle and right panels show top and bottom views of the complex, respectively, to highlight the overall architecture and subunit organization. (c) The left panel displays subunit A of GroEL bound to γATP (purple), with a boxed region indicating the ATPase active site. The right panel highlights this region in detail, showing the molecular surface enveloping the bound γATP. Key residues involved in ATP hydrolysis are labeled, including Lys51 (involved in ATP phosphate binding), Asp87 and Asp97 (which coordinate the essential Mg2+ ion and help position water for nucleophilic attack), Asp398 (which contributes to allosteric signaling and conformational changes) and Gly414 (which provides structural flexibility for proper positioning of catalytic residues). |
![[Figure 8]](ai5014fig8.jpg)
 | STRUCTURAL BIOLOGY |
ISSN: 2059-7983
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