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 heteronuclear Overhauser effects were determined at different temperatures for Escherichia coli SlyD (EcSlyD) and for Thermus thermophilus SlyD (TtSlyD). With the well established extended Lipari-Szabo approach, the order parameter, S(2), the internal correlation time, ?(e), the exchange rate, R(ex), of the backbone amide protons, and the overall molecular tumbling time, ?(m), were determined. The study was extended to a relaxation analysis of the peptide bound state for both SlyD species. We found highly different relaxation and dynamic behavior of the two domains for free SlyD. Surprisingly, in the presence of a substrate for the chaperone domain, the ps-to-ns dynamics in the remote center of the prolyl-peptidyl cis/trans isomerization domain increases. We observed this crosstalk between the two domains for both EcSlyD and TtSlyD.
[NMR paper] Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Related Articles Folding and domain-domain interactions of the chaperone PapD measured by 19F NMR.
Biochemistry. 2004 Nov 2;43(43):13775-86
Authors: Bann JG, Frieden C
The folding of the two-domain bacterial chaperone PapD has been studied to develop an understanding of the relationship between individual domain folding and the formation of domain-domain interactions. PapD contains six phenylalanine residues, four in the N-terminal domain and two in the...
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11-24-2010 10:03 PM
[NMR paper] Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with w
Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Related Articles Solvent interaction of a Hsp70 chaperone substrate-binding domain investigated with water-NOE NMR experiments.
Biochemistry. 2003 Sep 30;42(38):11100-8
Authors: Cai S, Stevens SY, Budor AP, Zuiderweg ER
The interaction of solvent of the substrate binding domain of the bacterial heat shock 70 chaperone protein DnaK was studied in its apo form and with bound hydrophobic substrate peptide, using refined nuclear magnetic...
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11-24-2010 09:16 PM
[NMR paper] NMR solution structure and dynamics of the peptidyl-prolyl cis-trans isomerase domain
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.
Related Articles 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
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...
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11-24-2010 08:49 PM
[NMR paper] Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
Related Articles Analysis of slow interdomain motion of macromolecules using NMR relaxation data.
J Am Chem Soc. 2001 May 2;123(17):3953-9
Authors: Baber JL, Szabo A, Tjandra N
The interpretation of NMR relaxation data for macromolecules possessing slow interdomain motions is considered. It is shown how the "extended model-free approach" can be used to analyze (15)N backbone relaxation data acquired at three different field strengths for Xenopus Ca(2+)-ligated...
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11-19-2010 08:32 PM
[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 paper] Direct determination of changes of interdomain orientation on ligation: use of the or
Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32).
Related Articles Direct determination of changes of interdomain orientation on ligation: use of the orientational dependence of 15N NMR relaxation in Abl SH(32).
Biochemistry. 1999 Aug 10;38(32):10225-30
Authors: Fushman D, Xu R, Cowburn D
The relative orientation and motions of domains within many proteins are key to the control of multivalent recognition, or the assembly of protein-based cellular...
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11-18-2010 08:31 PM
[NMR paper] NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain:
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Related Articles NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction.
Biochemistry. 1998 Jun 2;37(22):7929-40
Authors: Wang H, Kurochkin AV, Pang Y, Hu W, Flynn GC, Zuiderweg ER
The solution structure of the 21 kDa substrate-binding domain of the Escherichia coli Hsp70-chaperone protein DnaK (DnaK 386-561) has been determined to a precision...
NMR relaxation unravels interdomain crosstalk of the two domain prolyl isomerase and chaperone SlyD.
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