Related ArticlesBackbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase ?-subunit from solution-state NMR.
J Biomol NMR. 2020 May 15;:
Authors: Sakhrani VV, Hilario E, Caulkins BG, Hatcher-Skeers ME, Fan L, Dunn MF, Mueller LJ
Abstract
Backbone assignments for the isolated ?-subunit of Salmonella typhimurium tryptophan synthase (TS) are reported based on triple resonance solution-state NMR experiments on a uniformly 2H,13C,15N-labeled sample. From the backbone chemical shifts, secondary structure and random coil index order parameters (RCI-S2) are predicted. Titration with the 3-indole-D-glycerol 3'-phosphate analog, N-(4'-trifluoromethoxybenzenesulfonyl)-2-aminoethyl phosphate (F9), leads to chemical shift perturbations indicative of conformational changes from which an estimate of the dissociation constant is obtained. Comparisons of the backbone chemical-shifts, RCI-S2 values, and site-specific relaxation times with and without F9 reveal allosteric changes including modulation in secondary structures and loop rigidity induced upon ligand binding. A comparison is made to the X-ray crystal structure of the ?-subunit in the full TS ???? bi-enzyme complex and to two new X-ray crystal structures of the isolated TS ?-subunit reported in this work.
PMID: 32415580 [PubMed - as supplied by publisher]
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase α-subunit from solution-state NMR
Abstract
Backbone assignments for the isolated α-subunit of Salmonella typhimurium tryptophan synthase (TS) are reported based on triple resonance solution-state NMR experiments on a uniformly 2H,13C,15N-labeled sample. From the backbone chemical shifts, secondary structure and random coil index order parameters (RCI-S2) are predicted. Titration with the 3-indole-d-glycerol 3�-phosphate analog,...
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[NMR paper] Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--production.springer.de-OnlineResources-Logos-springerlink.gif Related Articles Backbone ¹H, ¹³C, ¹?N NMR assignments of yeast OMP synthase in unliganded form and in complex with orotidine 5'-monophosphate.
Biomol NMR Assign. 2014 Apr;8(1):103-8
Authors: Hansen MR, Harris R, Barr EW, Cheng H, Girvin ME, Grubmeyer C
Abstract
The...
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Protonation States of the Tryptophan Synthase Internal Aldimine Active Site from Solid-State NMR Spectroscopy: Direct Observation of the Protonated Schiff Base Linkage to Pyridoxal-5?-Phosphate
Protonation States of the Tryptophan Synthase Internal Aldimine Active Site from Solid-State NMR Spectroscopy: Direct Observation of the Protonated Schiff Base Linkage to Pyridoxal-5?-Phosphate
Bethany G. Caulkins, Baback Bastin, Chen Yang, Thomas J. Neubauer, Robert P. Young, Eduardo Hilario, Yu-ming M. Huang, Chia-en A. Chang, Li Fan, Michael F. Dunn, Michael J. Marsella and Leonard J. Mueller
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja506267d/aop/images/medium/ja-2014-06267d_0003.gif
Journal of the American Chemical Society...
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[NMR paper] Cardiolipin Interaction with Subunit c of ATP synthase: Solid-state NMR Characterization.
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Biochim Biophys Acta. 2014 Aug 25;
Authors: Laage S, Tao Y, McDermott AE
Abstract
The interaction of lipids with subunit c from F1Fo ATP synthase are studied by biophysical methods. Subunit c from both Escherichia coli and Streptococcus pneumoniae interact and copurify with cardiolipin. Solid state NMR data on oligomeric rings of Fo...
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08-30-2014 11:00 PM
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
Structure analysis of membrane-reconstituted subunit c-ring of E. coli H+-ATP synthase by solid-state NMR.
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J Biomol NMR. 2010 Sep;48(1):1-11
Authors: Todokoro Y, Kobayashi M, Sato T, Kawakami T, Yumen I, Aimoto S, Fujiwara T, Akutsu H
The subunit c-ring of H(+)-ATP synthase (F(o) c-ring) plays an essential role in the proton translocation across a membrane driven by the electrochemical potential. To understand its structure and function, we...
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[NMR paper] Solution NMR structure and backbone dynamics of the PsaE subunit of photosystem I fro
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Biochemistry. 2002 Nov 26;41(47):13902-14
Authors: Barth P, Savarin P, Gilquin B, Lagoutte B, Ochsenbein F
PsaE is a small peripheral subunit of photosystem I (PSI) that is very accessible to the surrounding medium. It plays an essential role in optimizing the interactions with the soluble electron...
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[NMR paper] Subunit-specific backbone NMR assignments of a 64 kDa trp repressor/DNA complex: a ro
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J Biomol NMR. 1998 Apr;11(3):307-18
Authors: Shan X, Gardner KH, Muhandiram DR, Kay LE, Arrowsmith CH
Deuterium decoupled, triple resonance NMR spectroscopy was used to analyze complexes of 2H, 15N, 13C labelled intact and (des2-7) trp repressor (delta 2-7 trpR) from E....
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11-17-2010 11:06 PM
[NMR paper] Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Esc
Comparison of backbone and tryptophan side-chain dynamics of reduced and oxidized Escherichia coli thioredoxin using 15N NMR relaxation measurements.
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Biochemistry. 1993 Jan 19;32(2):426-35
Authors: Stone MJ, Chandrasekhar K, Holmgren A, Wright PE, Dyson HJ
The backbone and tryptophan side-chain dynamics of both the reduced and oxidized forms of uniformly 15N-labeled Escherichia...
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase ?-subunit from solution-state NMR.
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