Related ArticlesNMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli.
Biomol NMR Assign. 2015 Nov 2;
Authors: Huang CT, Hsu SD
Abstract
Trigger factor (TF) is a highly conserved multi-domain molecular chaperone in bacteria. It binds via its ribosome binding domain (RBD) to the ribosomal tunnel exit and facilitates co-translational folding of a broad range of protein substrates primarily through interactions with the substrate binding domain (SBD) adjacent to the RBD. Within the SBD, a peptidyl-prolyl cis-trans isomerase (PPIase) domain is inserted leading to an unusual domain insertion, which may provide stabilizing effect to the highly plastic SBD. Here we report the near complete NMR assignments of TF PPIase providing the basis for subsequent structural and folding in the context of the chaperone activity of TF.
PMID: 26527152 [PubMed - as supplied by publisher]
[NMR paper] NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Related Articles NMR assignments for the cis and trans forms of the hemolysin II C-terminal domain.
Biomol NMR Assign. 2013 Nov 15;
Authors: Kaplan AR, Maciejewski MW, Olson R, Alexandrescu AT
Abstract
Pathogenic bacteria secrete pore-forming toxins (PFTs) to selectively defend against immune cells and to break through cellular barriers in the host. Understanding how PFTs attack cell membranes is not only essential for therapeutic intervention but for...
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11-16-2013 03:14 PM
[NMR paper] NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles NMR backbone assignments of the tyrosine kinase domain of human fibroblast growth factor receptor 1.
Biomol NMR Assign. 2013 Jan 17;
Authors: Vajpai N, Schott AK, Vogtherr M, Breeze AL
Abstract
Members of the fibroblast growth factor receptor tyrosine kinase family (FGFR1-4) play an important role in many...
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02-03-2013 10:19 AM
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Segmental isotopic labeling of a 140 kDa dimeric multi-domain protein CheA from Escherichia coli by expressed protein ligation and protein trans-splicing
Abstract Segmental isotopic labeling is a powerful labeling tool to facilitate NMR studies of larger proteins by not only alleviating the signal overlap problem but also retaining features of uniform isotopic labeling. Although two approaches, expressed protein ligation (EPL) and protein trans-splicing (PTS), have been mainly used for segmental isotopic labeling, there has been no single example in which both approaches have been...
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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...
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08-13-2011 12:57 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] 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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11-19-2010 08:29 PM
[NMR paper] The NMR structure of the RNA binding domain of E. coli rho factor suggests possible R
The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Related Articles The NMR structure of the RNA binding domain of E. coli rho factor suggests possible RNA-protein interactions.
Nat Struct Biol. 1998 May;5(5):393-9
Authors: Briercheck DM, Wood TC, Allison TJ, Richardson JP, Rule GS
Rho protein is an essential hexameric RNA-DNA helicase that binds nascent mRNA transcripts and terminates transcription in a wide variety of eubacterial species. The NMR solution structure of the RNA binding...
NMR assignments of the peptidyl-prolyl cis-trans isomerase domain of trigger factor from E. coli.
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