1q6h
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Crystal structure of a truncated form of FkpA from Escherichia coli
OverviewOverview
The protein FkpA from the periplasm of Escherichia coli exhibits both, cis/trans peptidyl-prolyl isomerase (PPIase) and chaperone activities. The, crystal structure of the protein has been determined in three different, forms: as the full-length native molecule, as a truncated form lacking the, last 21 residues, and as the same truncated form in complex with the, immunosuppressant ligand, FK506. FkpA is a dimeric molecule in which the, 245-residue subunit is divided into two domains. The N-terminal domain, includes three helices that are interlaced with those of the other subunit, to provide all inter-subunit contacts maintaining the dimeric species. The, C-terminal domain, which belongs to the FK506-binding protein (FKBP), family, binds the FK506 ligand. The overall form of the dimer is V-shaped, and the different crystal structures reveal a flexibility in the relative, orientation of the two C-terminal domains located at the extremities of, the V. The deletion mutant FkpNL, comprising the N-terminal domain only, exists in solution as a mixture of monomeric and dimeric species, and, exhibits chaperone activity. By contrast, a deletion mutant comprising the, C-terminal domain only is monomeric, and although it shows PPIase, activity, it is devoid of chaperone function. These results suggest that, the chaperone and catalytic activities reside in the N and C-terminal, domains, respectively. Accordingly, the observed mobility of the, C-terminal domains of the dimeric molecule could effectively adapt these, two independent folding functions of FkpA to polypeptide substrates.
About this StructureAbout this Structure
1Q6H is a Single protein structure of sequence from Escherichia coli. Active as Peptidylprolyl isomerase, with EC number 5.2.1.8 Full crystallographic information is available from OCA.
ReferenceReference
Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity., Saul FA, Arie JP, Vulliez-le Normand B, Kahn R, Betton JM, Bentley GA, J Mol Biol. 2004 Jan 9;335(2):595-608. PMID:14672666
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