3zq0 | pdb_00003zq0

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

spinqualitylabelsall models 3zq0, resolution 9.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3zq0 is a 21 chain structure with sequence from Escherichia coli bl21 and Escherichia coli k-12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, MG Related: 3zpz, 3zq1 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. Visualizing GroEL/ES in the Act of Encapsulating a Folding Protein.,Chen DH, Madan D, Weaver J, Lin Z, Schroder GF, Chiu W, Rye HS Cell. 2013 Jun 6;153(6):1354-65. doi: 10.1016/j.cell.2013.04.052. PMID:23746846 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chaperonin

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