2NWC
A 3.02 angstrom crystal structure of wild-type apo GroEL in a monoclinic space group
Summary for 2NWC
| Entry DOI | 10.2210/pdb2nwc/pdb |
| Descriptor | 60 kDa chaperonin (1 entity in total) |
| Functional Keywords | chaperonin, hsp60, chaperone |
| Biological source | Escherichia coli |
| Cellular location | Cytoplasm (By similarity): Q1R3B6 |
| Total number of polymer chains | 14 |
| Total formula weight | 801647.06 |
| Authors | Kiser, P.D.,Lodowski, D.T.,Palczewski, K. (deposition date: 2006-11-14, release date: 2007-05-22, Last modification date: 2023-08-30) |
| Primary citation | Kiser, P.D.,Lodowski, D.T.,Palczewski, K. Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions Acta Crystallogr.,Sect.F, 63:457-461, 2007 Cited by PubMed Abstract: GroEL is a member of the ATP-dependent chaperonin family that promotes the proper folding of many cytosolic bacterial proteins. The structures of GroEL in a variety of different states have been determined using X-ray crystallography and cryo-electron microscopy. In this study, a 3.02 A crystal structure of the native GroEL complex from Escherichia coli is presented. The complex was purified and crystallized in the absence of potassium ions, which allowed evaluation of the structural changes that may occur in response to cognate potassium-ion binding by comparison to the previously determined wild-type GroEL structure (PDB code 1xck), in which potassium ions were observed in all 14 subunits. In general, the structure is similar to the previously determined wild-type GroEL crystal structure with some differences in regard to temperature-factor distribution. PubMed: 17554162DOI: 10.1107/S1744309107020295 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.02 Å) |
Structure validation
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