Literature summary for 5.6.1.7 extracted from

Saibil, H.R.; Fenton, W.A.; Clare, D.K.; Horwich, A.L.
Structure and allostery of the chaperonin GroEL (2013), J. Mol. Biol., 425, 1476-1487.

Search for more literature for 5.6.1.7

Activating Compound

Activating Compound	Comment	Organism	Structure
ATP	ATP is an allosteric ligand for GroEL, its binding promoting both cooperative (intra-ring) and anti-cooperative (inter-ring) actions. ATP serves as a substrate, undergoing hydrolysis during the reaction cycle to promote a unidirectional advance of the machine	Escherichia coli
GroES	an allosteric effector of ATP hydrolysis. GroES contact leads to large rigid-body apical movements that eject polypeptide into an enclosed folding chamber. Docking of GroES stabilizes the Rs-open state, taking this assembly to a more energetically stable state that is no longer reversible and that is committed to the further large movements to a final energetic minimum that is the fully domed end state	Escherichia coli

Crystallization (Commentary)

Crystallization (Comment)	Organism
analysis of the X-ray crystal structures of GroEL and GroEL-GroES complexes in absence or presence of ATP, PDB IDs 1OEL and 1SVT, and of enzyme mutant E461K interface, PDB ID 2EU1	Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
E461K	site-directed mutagenesis, the inactive mutant of GroEL has a rearranged inter-ring interface, the normal 1:2 contacts of apposed equatorial domains in wild-type GroEL are replaced by 1:1 contacts in the mutant in the interfaces	Escherichia coli
F44W	site-directed mutagenesis, slower phases following addition of ATP to tryptophan-modified GroEL mutant	Escherichia coli
R231W	site-directed mutagenesis, apical domain mutation, slower phases following addition of ATP to tryptophan-modified GroEL mutant	Escherichia coli
Y485W	site-directed mutagenesis, equatorial ring mutation, slower phases following addition of ATP to tryptophan-modified GroEL mutant	Escherichia coli

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	cooperativity in GroEL, an allosteric enzyme complex, kinetic analysis, overview. Structural basis of negative cooperativity between rings. GroES is an allosteric effector of ATP hydrolysis	Escherichia coli

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Mg2+	required	Escherichia coli

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
57000	-	14 * 57000	Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + H2O + a folded polypeptide	Escherichia coli	-	ADP + phosphate + an unfolded polypeptide	-	?

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P0A6F5	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
ATP + H2O + a folded polypeptide	-	Escherichia coli	ADP + phosphate + an unfolded polypeptide	-	?
ATP + H2O + a folded polypeptide	ATP is an allosteric ligand for GroEL, its binding promoting both cooperative (intra-ring) and anti-cooperative (inter-ring) actions. ATP serves as a substrate, undergoing hydrolysis during the reaction cycle to promote a unidirectional advance of the machine. Inter-ring contacts in the ATPase cycle, modeling, overview	Escherichia coli	ADP + phosphate + an unfolded polypeptide	-	?

Subunits

Subunits	Comment	Organism
More	GroEL is composed of multiple identical protomers, 14 in all, arranged in a symmetric fashion as two back-to-back seven-member rings, rotational symmetry of the rings and symmetry between rings, involving seven 2fold symmetry axes between subunits in the apposing rings, producing an overall symmetry of D7. Each GroEL protomer is composed of two major domains, an equatorial domain at the waistline of the cylinder and an apical domain at the terminal end, covalently connected by a smaller intermediate domain that is hinged at its top and bottom aspects to allow for rigid-body movements. Each equatorial domain houses an ATP binding pocket, and seven of these domains contact each other side by side in each ring. The two rings contact each other back to back in a staggered fashion across the equatorial plane, forming a platform on which the other two domains of the machine undergo major movements in response to ATP binding and hydrolysis The equatorial domains themselves also undergo subtle cooperative movements during the reaction cycle, responsible for the asymmetric behavior of the machine, dictating that only one ring is folding active at a time. GroEL uses its apical domains and central cavity, remote from the ATP binding pocket, to supply kinetic assistance to polypeptide folding	Escherichia coli
tetradecamer	14 * 57000	Escherichia coli

Synonyms

Synonyms	Comment	Organism
chaperonin GroEL	-	Escherichia coli

General Information

General Information	Comment	Organism
additional information	the allosteric machine movements are choreographed by ATP binding, which triggers concerted tilting and twisting of subunit domains. These movements distort the ring of hydrophobic binding sites and split it apart, potentially unfolding the multiply bound substrate, structural nature of the allosteric action of this double-ring machine. ATP is an allosteric ligand for GroEL, its binding promoting both cooperative (intra-ring) and anti-cooperative (inter-ring) actions. Each equatorial domain houses an ATP binding pocket, and seven of these domains contact each other side by side in each ring. The two rings contact each other back to back in a staggered fashion across the equatorial plane, forming a platform on which the other two domains of the machine undergo major movements in response to ATP binding and hydrolysis The equatorial domains themselves also undergo subtle cooperative movements during the reaction cycle, responsible for the asymmetric behavior of the machine, dictating that only one ring is folding active at a time. GroELuses its apical domains and central cavity, remote from the ATP binding pocket, to supply kinetic assistance to polypeptide folding, allosteric structural changes in an ATP-bound GroEL ring, detailed structure-function and kinetic analysis, overview	Escherichia coli
physiological function	chaperonin GroEL is a protein folding machine. Chaperonins are intricate allosteric machines formed of two back-to-back, stacked rings of subunits presenting end cavities lined with hydrophobic binding sites for nonnative polypeptides. Once bound, substrates are subjected to forceful, concerted movements that result in their ejection from the binding surface and simultaneous encapsulation inside a hydrophilic chamber that favors their folding	Escherichia coli

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Release 2023.1 (January 2023)