Structural basis of the interaction between cyclodipeptide synthases and aminoacylated tRNA substrates.

Bourgeois G, Seguin J, Babin M, Gondry M, Mechulam Y, Schmitt E, RNA 26(11):1589-1602 (2020) Europe PMC

SASDJT4 – Complex of Candidatus Glomeribacter gigasporarum cyclodipeptide synthase (Cglo-CDPS) with Phe-tRNAPhe

Candidatus Glomeribacter gigasporarum cyclodipeptide synthase
E. coli Phe-tRNAPhe
MWexperimental 53 kDa
MWexpected 59 kDa
VPorod 77 nm3
log I(s) 4.96×10-2 4.96×10-3 4.96×10-4 4.96×10-5
Candidatus Glomeribacter gigasporarum cyclodipeptide synthase E. coli Phe-tRNAPhe small angle scattering data  s, nm-1
ln I(s)
Candidatus Glomeribacter gigasporarum cyclodipeptide synthase E. coli Phe-tRNAPhe Guinier plot ln 4.97×10-2 Rg: 3.3 nm 0 (3.3 nm)-2 s2
(sRg)2I(s)/I(0)
Candidatus Glomeribacter gigasporarum cyclodipeptide synthase E. coli Phe-tRNAPhe Kratky plot 1.104 0 3 sRg
Dmax: 14 nm

Data validation


There are no models related to this curve.

Synchrotron SAXS data measured from cyclodipeptide synthase bound to Phe-tRNAPhe in 10 mM MOPS pH6.7;,200 mM NaCl, 8 mM MgCl2 were collected on the SWING beam line at SOLEIL (Saint-Aubin, France) using a Eiger 4M detector at a wavelength of λ = 0.1033 nm (I(s) vs s, where s = 4πsinθ/λ, and 2θ is the scattering angle). In-line size-exclusion chromatography (SEC) SAS was employed. The SEC parameters were as follows: A sample was injected onto a GE Superdex 200 Increase 3.2/300 column at 15°C. The data were normalized to the intensity of the transmitted beam and radially averaged; the scattering of the solvent-blank was subtracted.

Sample injection concentration, UNKNOWN; Sample injection volume, UNKNOWN; SEC-column flow rate, UNKNOWN; Sample detector distance, UNKNOWN.

Candidatus Glomeribacter gigasporarum cyclodipeptide synthase (Cglo-CDPS)
Mol. type   Protein
Organism   Candidatus Glomeribacter gigasporarum
Olig. state   Monomer
Mon. MW   34.2 kDa
 
UniProt   G2JBB2 (2-291)
Sequence   FASTA
 
E. coli Phe-tRNAPhe (E. coli Phe-tRNAPhe)
Mol. type   RNA
Organism   Escherichia coli
Olig. state   Monomer
Mon. MW   24.5 kDa
Sequence   FASTA