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Structure of E. coli toxin RelE(R81A/R83A) mutant in the free state
Authors
Li, G., Zhang, Y., Inouye, M., Ikura, M.
Assembly
RelE
Entity
1. RelE (polymer, Thiol state: all free), 98 monomers, 11336.13 Da Detail

GSHMAYFLDF DERALKEWRK LGSTVREQLK KKLVEVLESP RIEANKLRGM PDCYKIKLRS SGYRLVYQVI DEKVVVFVIS VGKAEASEVY SEAVKRIL


Formula weight
11336.13 Da
Source organism
Escherichia coli
Exptl. method
solution NMR
Refine. method
torsion angle dynamics, simulated annealing
Data set
assigned_chemical_shifts
Chem. Shift Complete
Sequence coverage: 96.9 %, Completeness: 92.0 %, Completeness (bb): 94.0 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All92.0 % (1103 of 1199)95.2 % (599 of 629)87.2 % (410 of 470)94.0 % (94 of 100)
Backbone94.0 % (549 of 584)94.5 % (188 of 199)93.8 % (271 of 289)93.8 % (90 of 96)
Sidechain91.0 % (644 of 708)95.6 % (411 of 430)83.6 % (229 of 274)100.0 % (4 of 4)
Aromatic43.0 % (37 of 86)83.7 % (36 of 43) 0.0 % (0 of 42)100.0 % (1 of 1)
Methyl100.0 % (122 of 122)100.0 % (61 of 61)100.0 % (61 of 61)

1. RelE

GSHMAYFLDF DERALKEWRK LGSTVREQLK KKLVEVLESP RIEANKLRGM PDCYKIKLRS SGYRLVYQVI DEKVVVFVIS VGKAEASEVY SEAVKRIL

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05)


#NameIsotope labelingTypeConcentration
1RelE[U-13C; U-15N]0.5 (±0.1) mM
2sodium phosphatenatural abundance25 mM
3sodium chloridenatural abundance500 mM
4DTTnatural abundance1 mM
5sodium azidenatural abundance0.5 mM
Sample #2

Solvent system 100% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05)


#NameIsotope labelingTypeConcentration
6RelE[U-13C; U-15N]0.5 (±0.1) mM
7sodium phosphatenatural abundance25 mM
8sodium chloridenatural abundance500 mM
9DTTnatural abundance1 mM
10sodium azidenatural abundance0.5 mM

LACS Plot; CA
Referencing offset: 0.06 ppm, Outliers: 2 Detail
LACS Plot; CB
Referencing offset: 0.06 ppm, Outliers: 2 Detail
LACS Plot; HA
Referencing offset: 0.0 ppm, Outliers: 2 Detail
LACS Plot; CO
Referencing offset: -0.06 ppm, Outliers: 1 Detail
Protein Blocks Logo
Calculated from 20 models in PDB: 2KC9, Strand ID: A Detail


Release date
2009-04-21
Citation
Inhibitory mechanism of Escherichia coli RelE-RelB toxin-antitoxin module involves a helix displacement near an mRNA interferase active site
Li, G., Zhang, Y., Inouye, M., Ikura, M.
J. Biol. Chem. (2009), 284, 14628-14636, PubMed 19297318 , DOI 10.1074/jbc.M809656200 ,
Entries sharing articles BMRB: 2, Swiss-Prot: 2 entries Detail
  BMRB: 16065 released on 2009-04-21
    Title Structure of E. coli toxin RelE(R81A/R83A)mutant in complex with antitoxin RelBc (K47-L79) peptide
  BMRB: 16067 released on 2009-04-21
    Title Backbone assignment of RelB antitoxin C-terminal peptide (RelBc) in the RelE-free state
  Swiss-Prot: P0C077 released on 1988-04-01
    Title RELE_ECOLI Entity mRNA interferase RelE
  Swiss-Prot: P0C079 released on 1988-04-01
    Title RELB_ECOLI Entity Antitoxin RelB
Related entities 1. RelE, : 1 : 1 : 7 : 5 entities Detail
Interaction partners 1. RelE, : 13 interactors Detail
Experiments performed 11 experiments Detail
NMR combined restraints 5 contents Detail
Keywords mRNA interferase, RelE, Toxin, translation inhibitor