(Q27639120)

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NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein

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NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain of the trigger factor from Mycoplasma genitalium compared to FK506-binding protein (English)

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Mycoplasma genitalium

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protein structure

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solution structure

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based on heuristic

inferred from title

Christian Griesinger

8

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Heinz Rüterjans

7

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author name string

Martin Vogtherr

1

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Doris M Jacobs

2

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Tatjana N Parac

3

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Marcus Maurer

4

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Andreas Pahl

5

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Krishna Saxena

6

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Klaus M Fiebig

9

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language of work or name

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publication date

10 May 2002

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Journal of Molecular Biology

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318

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4

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1097-115

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Peptidyl-prolyl cis-trans isomerases, a superfamily of ubiquitous folding catalysts

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Protein folding in the cytosol: chaperonin-dependent and -independent mechanisms

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Molecular chaperones in cellular protein folding

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NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans isomerase domain of the mitotic regulator hPin1 but indicates a different functionality of the protein

1 reference

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Trigger factor: a soluble protein that folds pro-OmpA into a membrane-assembly-competent form

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ProOmpA is stabilized for membrane translocation by either purified E. coli trigger factor or canine signal recognition particle

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A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor

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Escherichia coli trigger factor is a prolyl isomerase that associates with nascent polypeptide chains.

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Cooperation of enzymatic and chaperone functions of trigger factor in the catalysis of protein folding

1 reference

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The amino-terminal 118 amino acids of Escherichia coli trigger factor constitute a domain that is necessary and sufficient for binding to ribosomes.

1 reference

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Modular structure of the trigger factor required for high activity in protein folding.

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Recognition of protein substrates by the prolyl isomerase trigger factor is independent of proline residues

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Overexpression of trigger factor prevents aggregation of recombinant proteins in Escherichia coli

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Trigger factor and DnaK cooperate in folding of newly synthesized proteins.

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Polypeptide flux through bacterial Hsp70: DnaK cooperates with trigger factor in chaperoning nascent chains

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Trigger factor associates with GroEL in vivo and promotes its binding to certain polypeptides

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Trigger factor is induced upon cold shock and enhances viability of Escherichia coli at low temperatures

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The Minimal Gene Complement of Mycoplasma genitalium

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Prolyl isomerases in a minimal cell. Catalysis of protein folding by trigger factor from Mycoplasma genitalium.

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Identification of the prolyl isomerase domain of Escherichia coli trigger factor

1 reference

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An 11.8 kDa proteolytic fragment of the E. coli trigger factor represents the domain carrying the peptidyl-prolyl cis/trans isomerase activity.

1 reference

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An internal FK506-binding domain is the catalytic core of the prolyl isomerase activity associated with the Bacillus subtilis trigger factor

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Trigger factor, one of the Escherichia coli chaperone proteins, is an original member of the FKBP family

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Correlating backbone amide and side chain resonances in larger proteins by multiple relayed triple resonance NMR

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Assignment of the 1H, 13C and 15N resonances of the PPIase domain of the trigger factor from Mycoplasma genitalium

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Structural and dynamical properties of a denatured protein. Heteronuclear 3D NMR experiments and theoretical simulations of lysozyme in 8 M urea

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Validation of Protein Structure from Anisotropic Carbonyl Chemical Shifts in a Dilute Liquid Crystalline Phase

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Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

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φ Angle Restraints in Protein Backbones from Dipole−Dipole Cross-Correlation between1HN−15N and1HN−1HαVectors

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X-ray structures of small ligand-FKBP complexes provide an estimate for hydrophobic interaction energies

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Atomic structure of FKBP-FK506, an immunophilin-immunosuppressant complex

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Atomic structures of the human immunophilin FKBP-12 complexes with FK506 and rapamycin

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β-Sheet topology and the relatedness of proteins

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Structural and functional analysis of the mitotic rotamase Pin1 suggests substrate recognition is phosphorylation dependent

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Binding specificity of Escherichia coli trigger factor

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Mechanism for the rotamase activity of FK506 binding protein from molecular dynamics simulations

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A mechanism for rotamase catalysis by the FK506 binding protein (FKBP)

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Sequence diversification of the FK506-binding proteins in several different genomes

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X-ray structure of calcineurin inhibited by the immunophilin-immunosuppressant FKBP12-FK506 complex

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Use of organic solvents and small molecules for locating binding sites on proteins in solutions

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Mapping the stereospecificity of peptidyl prolyl cis/trans isomerases

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10.1016/S0022-2836(02)00112-2

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release_kto733nndrgyfg3jltbb43zsmm

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