Related ArticlesNMR 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
Authors: Vogtherr M, Jacobs DM, Parac TN, Maurer M, Pahl A, Saxena K, Rüterjans H, Griesinger C, Fiebig KM
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.
NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD.
NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD.
NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD.
Biochim Biophys Acta. 2011 Jul;1814(7):873-81
Authors: Kovermann M, Zierold R, Haupt C, Löw C, Balbach J
The dynamics of the two domain prolyl-peptidyl cis/trans isomerase and chaperone SlyD was studied on a ps-to-ns time scale to correlate dynamic changes with the catalytic function. (15)N transversal and longitudinal relaxation rates as well as...
[NMR paper] Solution-state NMR investigations of triosephosphate isomerase active site loop motio
Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
Related Articles Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
J Mol Biol. 2001 Jun 29;310(1):271-80
Authors: Rozovsky S, Jogl G, Tong L, McDermott AE
Product release is partially rate determining in the isomerization reaction catalyzed by Triosephosphate Isomerase, the conversion of dihydroxyacetone...
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[NMR paper] NMR solution structure of hPar14 reveals similarity to the peptidyl prolyl cis/trans
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.
Related Articles 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.
J Mol Biol. 2000 Aug 25;301(4):1003-17
Authors: Sekerina E, Rahfeld JU, Müller J, Fanghänel J, Rascher C, Fischer G, Bayer P
The 131-amino acid residue...
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NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6.
J Biomol NMR. 2010 Aug;47(4):283-8
Authors: Chen J, Li Q, Liu CC, Zhou B, Bu G, Wang J
NMR structure note: solution structure of the core domain of MESD that is essential f
NMR structure note: solution structure of the core domain of MESD that is essential for proper folding of LRP5/6
Content Type Journal Article
DOI 10.1007/s10858-010-9426-8
Authors
Jianglei Chen, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Qianqian Li, Wayne State University Department of Biochemistry and Molecular Biology, School of Medicine Detroit MI 48201 USA
Chia-Chen Liu, Washington University Departments of Pediatrics, and Cell Biology and Physiology, School of Medicine St. Louis MO 63110 USA
NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain
Linear Mode
