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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.
J Mol Biol. 2002 May 10; 318(4):1097-115.JM

Abstract

We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A. As predicted, the PPIase domain of the trigger factor adopts the FK506 binding protein (FKBP) fold. Furthermore, our NMR relaxation data indicate that the dynamic behavior of the trigger factor PPIase domain and of FKBP are similar. Structural variations when compared to FKBP exist in the flap region and within the bulges of strand 5 of the beta sheet. Although the active-site crevice is similar to that of FKBP, subtle steric variations in this region can explain why FK506 does not bind to the trigger factor. Sequence variability (27% identity) between trigger factor and FKBP results in significant differences in surface charge distribution and the absence of the first strand of the central beta sheet. Our data indicate, however, that this strand may be partially structured as "nascent" beta strand. This makes the trigger factor PPIase domain the most minimal representative of the FKBP like protein family of PPIases.

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Authors+Show Affiliations

Vogtherr M
Institut für Organische Chemie der Universität Frankfurt, Marie-Curie-Str. 11, 60439 Frankfurt, Germany.
Jacobs DM
No affiliation info available
Parac TN
No affiliation info available
Maurer M
No affiliation info available
Pahl A
No affiliation info available
Saxena K
No affiliation info available
Rüterjans H
No affiliation info available
Griesinger C
No affiliation info available
Fiebig KM
No affiliation info available

MeSH

Amino Acid SequenceBinding SitesCatalytic DomainDNA PrimersEscherichia coliHistidineHydrogen BondingIsomerismModels, MolecularMolecular Sequence DataMolecular StructureMycoplasmaNuclear Magnetic Resonance, BiomolecularPeptidylprolyl IsomeraseProtein BindingProtein ConformationProtein FoldingProtein Structure, TertiaryRecombinant Fusion ProteinsTacrolimus Binding Proteins

Pub Type(s)

Journal Article

Language

eng

PubMed ID

12054805

Citation

Vogtherr, Martin, et al. "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." Journal of Molecular Biology, vol. 318, no. 4, 2002, pp. 1097-115.
Vogtherr M, Jacobs DM, Parac TN, et al. 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. J Mol Biol. 2002;318(4):1097-115.
Vogtherr, M., Jacobs, D. M., Parac, T. N., Maurer, M., Pahl, A., Saxena, K., Rüterjans, H., Griesinger, C., & Fiebig, K. M. (2002). 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. Journal of Molecular Biology, 318(4), 1097-115.
Vogtherr M, et al. 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. J Mol Biol. 2002 May 10;318(4):1097-115. PubMed PMID: 12054805.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - 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. AU - Vogtherr,Martin, AU - Jacobs,Doris M, AU - Parac,Tatjana N, AU - Maurer,Marcus, AU - Pahl,Andreas, AU - Saxena,Krishna, AU - Rüterjans,Heinz, AU - Griesinger,Christian, AU - Fiebig,Klaus M, PY - 2002/6/11/pubmed PY - 2002/6/28/medline PY - 2002/6/11/entrez SP - 1097 EP - 115 JF - Journal of molecular biology JO - J Mol Biol VL - 318 IS - 4 N2 - We have solved the solution structure of the peptidyl-prolyl cis-trans isomerase (PPIase) domain of the trigger factor from Mycoplasma genitalium by homo- and heteronuclear NMR spectroscopy. Our results lead to a well-defined structure with a backbone rmsd of 0.23 A. As predicted, the PPIase domain of the trigger factor adopts the FK506 binding protein (FKBP) fold. Furthermore, our NMR relaxation data indicate that the dynamic behavior of the trigger factor PPIase domain and of FKBP are similar. Structural variations when compared to FKBP exist in the flap region and within the bulges of strand 5 of the beta sheet. Although the active-site crevice is similar to that of FKBP, subtle steric variations in this region can explain why FK506 does not bind to the trigger factor. Sequence variability (27% identity) between trigger factor and FKBP results in significant differences in surface charge distribution and the absence of the first strand of the central beta sheet. Our data indicate, however, that this strand may be partially structured as "nascent" beta strand. This makes the trigger factor PPIase domain the most minimal representative of the FKBP like protein family of PPIases. SN - 0022-2836 UR - https://www.unboundmedicine.com/medline/citation/12054805/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_ L2 - https://linkinghub.elsevier.com/retrieve/pii/S0022-2836(02)00112-2 DB - PRIME DP - Unbound Medicine ER -