6OSO

The crystal structure of the isolate tryptophan synthase alpha-chain from Salmonella enterica serovar typhimurium at 1.75 Angstrom resolution

Summary for 6OSO

• Entry DOI: 10.2210/pdb6oso/pdb
• Related: 1V7Y 1WQ5 1XC4 1XCF 2DZP 2EKC 3THA 3VND 5KMY 5N2P 6OUY
• Descriptor: Tryptophan synthase alpha chain, SULFATE ION, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: tryptophan synthase, alpha-chain, wild-type, lyase, recombinant protein
• Biological source: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2
• Total number of polymer chains: 1
• Total formula weight: 29758.15

Authors

Hilario, E.,Dunn, M.F.,Mueller, L.,Chang, C.,Fan, L. (deposition date: 2019-05-01, release date: 2020-05-06, Last modification date: 2023-10-11)

Primary citation

Sakhrani, V.V.,Hilario, E.,Caulkins, B.G.,Hatcher-Skeers, M.E.,Fan, L.,Dunn, M.F.,Mueller, L.J.
Backbone assignments and conformational dynamics in the S. typhimurium tryptophan synthase alpha-subunit from solution-state NMR.
J.Biomol.Nmr, 74:341-354, 2020

PubMed 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 H,C,N-labeled sample. From the backbone chemical shifts, secondary structure and random coil index order parameters (RCI-S) 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-S 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 α-subunit in the full TS αββα bi-enzyme complex and to two new X-ray crystal structures of the isolated TS α-subunit reported in this work.

PubMed: 32415580
DOI: 10.1007/s10858-020-00320-2

Experimental method

X-RAY DIFFRACTION (1.75 Å)