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5.2.1.8: peptidylprolyl isomerase

This is an abbreviated version!
For detailed information about peptidylprolyl isomerase, go to the full flat file.

Word Map on EC 5.2.1.8

Reaction

peptidylproline (omega = 180)

Synonyms

12 kDa FKBP, 12.6 kDa FKBP, 13 kDa FKBP, 15 kDa FKBP, 19 kDa FK506-binding protein, 22 kDa FK506-binding protein, 25 kDa FKBP, 27 kDa membrane protein, 36 kDa FK506 binding protein, 40 kDa thylakoid lumen PPIase, 40 kDa thylakoid lumen rotamase, 51 kDa FK506-binding protein, 52 kDa FK506 binding protein, 54 kDa progesterone receptor-associated immunophilin, 65 kDa FK506-binding protein, At3g56070, CeCYP-16, CGI-124, Cgl0830, Chl-Mip, Cj0596, CPH, CTHT_0005290, Cwc27, Cyclophilin, Cyclophilin 18, cyclophilin 3, Cyclophilin 33, Cyclophilin A, Cyclophilin B, Cyclophilin C, Cyclophilin cyp2, cyclophilin H, cyclophilin hCyp-18, Cyclophilin homolog, cyclophilin J, Cyclophilin ScCypA, Cyclophilin ScCypB, Cyclophilin-10, Cyclophilin-11, Cyclophilin-40, Cyclophilin-60, cyclophilin-A, cyclophilin-D, Cyclophilin-like protein Cyp-60, Cyclophilin-related protein, Cyclosporin A-binding protein, Cyp, CYP-3, CYP-40, CYP-5, CYP-6, cyp-A, CYP-S1, Cyp1, Cyp18, Cyp19-3, Cyp2, CYP20-2, CYP20-3, Cyp3, Cyp3 PPIase, Cyp40, CyPA, CypA-1, CyPB, CyPJ, DDB_G0268618, Dod, EF0685, EF1534, EF2898, Estrogen receptor binding cyclophilin, FF1 antigen, FK506 binding protein 12, FK506 binding protein 35, FK506-binding protein, FKBP, FKBP 12, FKBP-12, FKBP-12.6, FKBP-13, FKBP-15, FKBP-19, FKBP-21, FKBP-22, FKBP-23, FKBP-25, FKBP-36, FKBP-51, FKBP-70, FkbP10, FKBP12, FKBP13, FKBP17, FKBP1B, FKBP22, FKBP25, FKBP3, FKBP33, FKBP35, FKBP38, FKBP51, FKBP52, FKBP52 protein, FKBP54, FKBP59, FKBP65, FKBP65RS, FKBP77, FklB, FkpA, h Par14, HBI, HcCYP, hCyP33, Histidine rich protein, hPar14, hPin1, HSP binding immunophilin, HSP90-binding immunophilin, Immunophilin FKBP12, Immunophilin FKBP12.6, Immunophilin FKBP36, Immunophilin FKBP65, Isomerase, peptidylprolyl cis-trans, L.p.Cyp18, Macrolide binding protein, Macrophage infectivity potentiator, mimicyp, MIP, mip-like peptidyl-prolyl cis-trans isomerase, More, MtFK, MtFKBP17, mzFKBP-66, Ng-MIP, NIMA-1, Nucleolar proline isomerase, OvCYP-16, p17.7, P31, P54, p59 protein, Par10, Par14, Par27, Par45, Parvulin, Parvulin 14, parvulin-like protein, parvulin-type peptidyl-prolyl isomerase, parvulin1 4, pCYP B, Peptide bond isomerase, peptidyl prolyl cis-trans isomerase, peptidyl prolyl isomerase-like protein 1, Peptidyl-prolyl cis-trans isomerase, peptidyl-prolyl cis-trans isomerase NIMA-interacting 1, Peptidyl-prolyl cis-trans isomerase plp, Peptidyl-prolyl cis-trans isomerase surA, peptidyl-prolyl cis/trans isomerase, Peptidyl-prolyl cis/trans isomerase EPVH, peptidyl-prolyl cis/trans isomerase NIMA-interacting 1, peptidyl-prolyl isomerase, peptidyl-prolyl isomerase 1, peptidylproline cis-trans-isomerase, peptidylprolyl cis,trans-isomerase, Peptidylprolyl cis-trans isomerase, peptidylprolyl cis/trans isomerase, peptidylprolyl isomerase, PfCyP, Pin1, PIN1-type parvulin 1, PIN1At, PinA, Planta-induced rust protein 28, Plp, PP2A phosphatase activator, PpiA, PPIase, PPIase Pin1, PPIase Pin4, PpiB, PPIC, PpiD, PPIE, PPIF, PPIG, PPIH, PPIL1, PPWD1, Proline rotamase, prolyl cis-trans isomerase, prolyl-peptidyl isomerase, protein phosphatase 2A phosphatase activator, Proteins, cyclophilins, Proteins, specific or class, cyclophilins, PrsA, Ptf1/Ess1, PtpA, PvFKBP35, Rapamycin-binding protein, Rapamycin-selective 25 kDa immunophilin, ROF2, Rotamase, Rotamase Pin1, Rotamase Pin4, Rotamase plp, S-cyclophilin, S1205-06, SAUSA300_0857, SCYLP, SDCCAG-10, sFkpA, SlrA, SLyD, SmCYP A, SmCYP B, Smp17.7, SP18, spliceosome-associated protein CWC27 homolog, SurA, TcFKBP18, TF, TLP20, trigger factor, TTHA0346, WHP, Ypa

ECTree

     5 Isomerases
         5.2 cis-trans-Isomerases
             5.2.1 cis-trans Isomerases (only sub-subclass identified to date)
                5.2.1.8 peptidylprolyl isomerase

Crystallization

Crystallization on EC 5.2.1.8 - peptidylprolyl isomerase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.0 A resolution. Computational model and comparison with human enzyme
molecular modeling of structure
purified recombinant His-tagged and SeMet-labeled enzyme, X-ray diffraction structure determination and analysis at 2.2-2.3 A resolution, homology modeling
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hanging-drop vapour-diffusion method, CYP-5, X-ray structure solved to a resolution of 1.75 A
two crystal forms are grown, hanging-drop vapour-diffusion method, solved to a resolution of 1.8 A
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NMR-study of enzyme and its complexes with substrates RNase A and reduced carboxymethylated bovine alpha-lactalbumin in solution. Molecular model of chaperone activity of enzyme
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
1.65 A resolution. The N-terminus of one isomerase domain is bound in the active site of a neighbouring isomerase molecule in a manner analogous to the substrate. This sequence binds to the active site of the enzyme, but cannot be turned over
2.0 A resolution, space group P3121
crystal structure of a complex between human spliceosomal cyclophilin H and a U4/U6 snRNP-60K peptide, hanging drop vapour diffusion method
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crystal structure of cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
crystal structure of cyclophilin A complexed with a binding site peptide from HIV-1 capsid protein
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crystal structures of cyclophilin A complexed with cyclosporin A and N-methyl-4-[(E)-2-butenyl]4,4-dimethylthreonine cyclosporin A
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crystallization of cyclophilin-tetrapeptide and cyclophilin-cyclosporin complexes
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hanging drop vapor diffusion method, using 25% (w/v) PEG MME 550, 0.1 M zinc acetate, 0.1 M MES at pH 6.5
in complex with inhibitor 1-[(1R,10S)-3,8-dioxa-14-azabicyclo[8.3.1]tetradec-14-yl]-3,3-dimethyl-1-oxopentan-2-one
in complex with inhibitor 4-phenyl-1-(3-pyridin-3-ylpropyl)butyl (2R)-1-[difluoro(3,4,5-trimethoxyphenyl)acetyl]piperidine-2-carboxylate. Fluorine atoms of inhibitor participate in discrete interactions with the Phe36 phenyl ring and the Tyr26 hydroxyl group of enzyme, with the latter resembling a moderate-to-weak hydrogen bond
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in complex with inhibitors (1R)-1,3-diphenyl-1-propyl (2S)-1-(3,3-dimethyl-1,2-dioxopentyl)-2-piperidinecarboxylate, (1S)-1-cyclohexyl-3-phenylpropyl (2R)-1-(3,3-dimethyl-2-oxopentanoyl)piperidine-2-carboxylate, (24aS)-17,17-dimethylhexadecahydropyrido[2,1-c][1,9,4]dioxazacyclohenicosine-1,14,18,19(3H,21H)-tetrone
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mutant K125A/E126A is crystallized by the hanging drop vapor diffusion method, using 2 M NH4SO4, 0.2 M NaCl, 0.1 M HEPES, pH 7.5
mutant P9Q/R13F/K17V/R18F in complex with 1-(pyridin-4-ylthio)bicyclo[3.3.1]nonan-3-one
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purified recombinant detagged wild-type and selenomethionine-labeled FKBP22, hanging drop vapor diffusion method, mixing of 0.002 ml of 3 mg/ml protein in 1 mM Tris/HCl, pH 7.2, and 0.05 mM CaCl2, with 0.001 ml of reservoir solution containing 0.1 M MES, 25% 1,2-propanediol, and 11-12% PEG 20000, pH 7.0-7.2, 1-2 weeks, X-ray diffraction structure determination and analysis at 1.9 A and 2.46 A resolution, respectively
recombinant enzyme
recombinant enzyme expressed in Escherichia coli
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recombinant protein, overall structure and analysis of cyclosporin A binding site
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sitting drop vapor diffusion method, using 20% (w/v) PEG 3350 and 0.2 M NaI
sitting drop vapor diffusion method, using 34% (w/v) PEG 8K, 0.2 M NH4SO4, and 0.1 M bis-Tris, pH 6.0
solution structure of protein determined by NMR spectroscopy
structure of a relatively protease-resistant N-terminal fragment containing the PPIase domain, t 2.0 A resolution. Residues Arg56, Phe61, Ile62, Gln64, Ala102, Asn103, Phe114, Glu122, Leu123 and His127 in beta-strands 3, 4 and 6, as well as in the extended loop connecting beta-strands 6 and 7, form the proline-binding pocket
structure of CYPJ at 2.0 A and in complex with cyclosporin A. Residues His43, Arg44 and Gln52 are conserved active-site residues located in the shallow pocket, and Arg44 displayes flexible conformation
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structure of human cyclophilin and its binding site for cyclophilin A determined by X-ray crystallography and NMR spectroscopy
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X-ray structure of a decameric cyclophilin-cyclosporin crystal complex
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X-ray structure of a monomeric cyclophilin A-cyclosporin A crystal complex at 2.1 A resolution
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crystal structure of murine cyclophilin C complexed with immunosuppressive drug cyclosporin A
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apo-enzyme PvFKBD35 free and in complex with the tetrapeptide substrate succinyl-Ala-Leu-Pro-Phe-p-nitroanilide, sitting-drop vapor diffusion method, mixing of 0.0002 ml of 10 mg/ml protein in 10 mM phosphate, pH 6.8, 137 mM NaCl, and 2.7 mM KCl, with 0.0002 ml of precipitant solution containing 0.1 M Tris-HCl, pH 8.5, 30% w/v PEG 4000, 0.2 M MgCl2, and and equilibration against 0.1 ml precipitant solution, 18°C, X-ray diffraction structure determination and analysis at 1.4 A and 1.65 A resolution, respectively
enzyme in reduced and oxidized state at 1.5 and 1.8 A resolution. Oxidized enzyme contains a disulfide bridge between C-terminal cysteines C122 and C126
1.3 A resolution crystal structure of the peptidyl-prolyl cis-trans isomerase domain
Thermochaetoides thermophila
crystal structures with the inhibitor FK506 bound to the FK506-binding domain, and with 15-residue-long peptides bound to either one or both domains. Substrates bind in a highly adaptable fashion to the insert-in-flap chaperone domain through beta-strand augmentation, and can bind to the FK506-binding domain
molecular modeling of structure
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