3ZQ1

Visualizing GroEL-ES in the Act of Encapsulating a Non-Native Substrate Protein

Summary for 3ZQ1

• Entry DOI: 10.2210/pdb3zq1/pdb
• Related: 3ZPZ 3ZQ0
• EMDB information: 2327
• Descriptor: 60 KDA CHAPERONIN, 10 KDA CHAPERONIN, MAGNESIUM ION, ... (4 entities in total)
• Functional Keywords: chaperone, rubisco, encapsulation
• Biological source: ESCHERICHIA COLI BL21; More
• Cellular location: Cytoplasm : P0A6F5 P0A6F9
• Total number of polymer chains: 21
• Total formula weight: 852454.53

Authors

Chen, D.-H.,Madan, D.,Weaver, J.,Lin, Z.,Schroder, G.F.,Chiu, W.,Rye, H.S. (deposition date: 2013-03-04, release date: 2013-06-19, Last modification date: 2024-05-08)

Primary citation

Chen, D.-H.,Madan, D.,Weaver, J.,Lin, Z.,Schroder, G.F.,Chiu, W.,Rye, H.S.
Visualizing Groel/Es in the Act of Encapsulating a Folding Protein
Cell(Cambridge,Mass.), 153:1354-, 2013

PubMed Abstract: The GroEL/ES chaperonin system is required for the assisted folding of many proteins. How these substrate proteins are encapsulated within the GroEL-GroES cavity is poorly understood. Using symmetry-free, single-particle cryo-electron microscopy, we have characterized a chemically modified mutant of GroEL (EL43Py) that is trapped at a normally transient stage of substrate protein encapsulation. We show that the symmetric pattern of the GroEL subunits is broken as the GroEL cis-ring apical domains reorient to accommodate the simultaneous binding of GroES and an incompletely folded substrate protein (RuBisCO). The collapsed RuBisCO folding intermediate binds to the lower segment of two apical domains, as well as to the normally unstructured GroEL C-terminal tails. A comparative structural analysis suggests that the allosteric transitions leading to substrate protein release and folding involve concerted shifts of GroES and the GroEL apical domains and C-terminal tails.

PubMed: 23746846
DOI: 10.1016/J.CELL.2013.04.052

Experimental method

ELECTRON MICROSCOPY (15.9 Å)