Literature summary for 5.2.1.8 extracted from

Saul, F.A.; Arie, J.P.; Vulliez-le Normand, B.; Kahn, R.; Betton, J.M.; Bentley, G.A.
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity (2004), J. Mol. Biol., 335, 595-608.

Crystallization (Commentary)

Crystallization (Comment)	Organism
three different forms: 1. crystals of the full length native molecule are obtained by sitting drop vapour diffusion method, 2. crystals of the truncated form lacking the last 21 residues are obtained by hanging drop vapour diffusion method 3. crystals of the truncated form lacking the last 21 residues in complex with the immunosuppressant ligand, FK506, are obtained by hanging drop vapour diffusion method	Escherichia coli

Crystallization (Comment)

Organism

three different forms: 1. crystals of the full length native molecule are obtained by sitting drop vapour diffusion method, 2. crystals of the truncated form lacking the last 21 residues are obtained by hanging drop vapour diffusion method 3. crystals of the truncated form lacking the last 21 residues in complex with the immunosuppressant ligand, FK506, are obtained by hanging drop vapour diffusion method

Escherichia coli

Protein Variants

Protein Variants	Comment	Organism
additional information	the deletion mutant comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and exhibits chaperone activity. The deletion mutant comprising the C-terminal domain only is monomeric, and although it shows peptidylprolyl isomerase activity, it is devoid of chaperone function	Escherichia coli

Localization

Localization	Comment	Organism	GeneOntology No.	Textmining
periplasm	-	Escherichia coli	-	-

Organism

Organism	UniProt	Comment	Textmining
Escherichia coli	P45523	-	-

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
additional information	the enzyme has peptidylprolyl isomerase activity and chaperone activity	Escherichia coli	?	-	?

Subunits

Subunits	Comment	Organism
dimer	245-residue subunit is divided into two domains, the overall form of the dimer is V-shaped, and the two C-terminal domains are located at the extremities of the V	Escherichia coli

Synonyms

Synonyms	Comment	Organism
FkpA	-	Escherichia coli