4V4O
Crystal Structure of the Chaperonin Complex Cpn60/Cpn10/(ADP)7 from Thermus Thermophilus
This is a non-PDB format compatible entry.
Summary for 4V4O
| Entry DOI | 10.2210/pdb4v4o/pdb |
| Descriptor | cpn60(GroEL), cpn10(GroES), MAGNESIUM ION, ... (5 entities in total) |
| Functional Keywords | chaperonin, chaperone, groel, groes, cpn60, cpn10, hsp60, hsp10, folding, adp, atp |
| Biological source | Thermus thermophilus More |
| Cellular location | Cytoplasm : P61490 P61492 |
| Total number of polymer chains | 42 |
| Total formula weight | 1782769.79 |
| Authors | Shimamura, T.,Koike-Takeshita, A.,Yokoyama, K.,Masui, R.,Murai, N.,Yoshida, M.,Taguchi, H.,Iwata, S. (deposition date: 2004-05-23, release date: 2014-07-09, Last modification date: 2024-03-20) |
| Primary citation | Shimamura, T.,Koike-Takeshita, A.,Yokoyama, K.,Masui, R.,Murai, N.,Yoshida, M.,Taguchi, H.,Iwata, S. Crystal structure of the native chaperonin complex from Thermus thermophilus revealed unexpected asymmetry at the cis-cavity STRUCTURE, 12:1471-1480, 2004 Cited by PubMed Abstract: The chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES (cis-cavity). We determined the crystal structure of the native GroEL-GroES-ADP homolog from Thermus thermophilus, with substrate proteins in the cis-cavity, at 2.8 A resolution. Twenty-four in vivo substrate proteins within the cis-cavity were identified from the crystals. The structure around the cis-cavity, which encapsulates substrate proteins, shows significant differences from that observed for the substrate-free Escherichia coli GroEL-GroES complex. The apical domain around the cis-cavity of the Thermus GroEL-GroES complex exhibits a large deviation from the 7-fold symmetry. As a result, the GroEL-GroES interface differs considerably from the previously reported E. coli GroEL-GroES complex, including a previously unknown contact between GroEL and GroES. PubMed: 15296740DOI: 10.1016/j.str.2004.05.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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