5OPX
Crystal structure of the GroEL mutant A109C in complex with GroES and ADP BeF2
Summary for 5OPX
| Entry DOI | 10.2210/pdb5opx/pdb |
| Descriptor | 60 kDa chaperonin, 10 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | chaperonin, chaperone |
| Biological source | Escherichia coli (strain K12) More |
| Total number of polymer chains | 28 |
| Total formula weight | 957338.51 |
| Authors | Yan, X.,Shi, Q.,Bracher, A.,Milicic, G.,Singh, A.K.,Hartl, F.U.,Hayer-Hartl, M. (deposition date: 2017-08-10, release date: 2018-01-10, Last modification date: 2024-10-23) |
| Primary citation | Yan, X.,Shi, Q.,Bracher, A.,Milicic, G.,Singh, A.K.,Hartl, F.U.,Hayer-Hartl, M. GroEL Ring Separation and Exchange in the Chaperonin Reaction. Cell, 172:605-617.e11, 2018 Cited by PubMed Abstract: The bacterial chaperonin GroEL and its cofactor, GroES, form a nano-cage for a single molecule of substrate protein (SP) to fold in isolation. GroEL and GroES undergo an ATP-regulated interaction cycle to close and open the folding cage. GroEL consists of two heptameric rings stacked back to back. Here, we show that GroEL undergoes transient ring separation, resulting in ring exchange between complexes. Ring separation occurs upon ATP-binding to the trans ring of the asymmetric GroEL:7ADP:GroES complex in the presence or absence of SP and is a consequence of inter-ring negative allostery. We find that a GroEL mutant unable to perform ring separation is folding active but populates symmetric GroEL:GroES complexes, where both GroEL rings function simultaneously rather than sequentially. As a consequence, SP binding and release from the folding chamber is inefficient, and E. coli growth is impaired. We suggest that transient ring separation is an integral part of the chaperonin mechanism. PubMed: 29336887DOI: 10.1016/j.cell.2017.12.010 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.64 Å) |
Structure validation
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