4PKN
Crystal structure of the football-shaped GroEL-GroES2-(ADPBeFx)14 complex containing substrate Rubisco
Summary for 4PKN
| Entry DOI | 10.2210/pdb4pkn/pdb |
| Related | 4PKO |
| Descriptor | 60 kDa chaperonin, 10 kDa chaperonin, ADENOSINE-5'-DIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | chaperonin, protein encapsulation, groel-groes2 "football" complex, rubisco, protein binding |
| Biological source | Escherichia coli More |
| Cellular location | Cytoplasm (By similarity): Q548M1 Q7BGE6 |
| Total number of polymer chains | 28 |
| Total formula weight | 956889.64 |
| Authors | Fei, X.,Ye, X.,Laronde-Leblanc, N.,Lorimer, G.H. (deposition date: 2014-05-15, release date: 2014-08-20, Last modification date: 2023-12-27) |
| Primary citation | Fei, X.,Ye, X.,LaRonde, N.A.,Lorimer, G.H. Formation and structures of GroEL:GroES2 chaperonin footballs, the protein-folding functional form. Proc.Natl.Acad.Sci.USA, 111:12775-12780, 2014 Cited by PubMed Abstract: The GroE chaperonins assist substrate protein (SP) folding by cycling through several conformational states. With each cycle the SP is, in turn, captured, unfolded, briefly encapsulated (t1/2 ∼ 1 s), and released by the chaperonin complex. The protein-folding functional form is the US-football-shaped GroEL:GroES2 complex. We report structures of two such "football" complexes to ∼ 3.7-Å resolution; one is empty whereas the other contains encapsulated SP in both chambers. Although encapsulated SP is not visible on the electron density map, using calibrated FRET and order-of-addition experiments we show that owing to SP-catalyzed ADP/ATP exchange both chambers of the football complex encapsulate SP efficiently only if the binding of SP precedes that of ATP. The two rings of GroEL thus behave as a parallel processing machine, rather than functioning alternately. Compared with the bullet-shaped GroEL:GroES1 complex, the GroEL:GroES2 football complex differs conformationally at the GroEL-GroES interface and also at the interface between the two GroEL rings. We propose that the electrostatic interactions between the ε-NH(3+) of K105 of helix D in one ring with the negatively charged carboxyl oxygen of A109 at the carboxyl end of helix D of the other ring provide the structural basis for negative inter-ring cooperativity. PubMed: 25136110DOI: 10.1073/pnas.1412922111 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.66 Å) |
Structure validation
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