Structural highlights
Function
[CH60_ECOUT] Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions.,Kiser PD, Lodowski DT, Palczewski K Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:17554162[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kiser PD, Lodowski DT, Palczewski K. Purification, crystallization and structure determination of native GroEL from Escherichia coli lacking bound potassium ions. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Jun 1;63(Pt, 6):457-61. Epub 2007 May 5. PMID:17554162 doi:10.1107/S1744309107020295
