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Structure of E. coli toxin RelE(R81A/R83A)mutant in complex with antitoxin RelBc (K47-L79) peptide
Authors
Li, G., Zhang, Y., Inouye, M., Ikura, M.
Assembly
RelE:RelBc complex
Entity
1. RelE (polymer, Thiol state: all free), 98 monomers, 11336.13 Da Detail

GSHMAYFLDF DERALKEWRK LGSTVREQLK KKLVEVLESP RIEANKLRGM PDCYKIKLRS SGYRLVYQVI DEKVVVFVIS VGKAEASEVY SEAVKRIL


2. RelBc (polymer, Thiol state: not present), 36 monomers, 4128.639 Da Detail

GSHKQTLLSD EDAELVEIVK ERLRNPKPVR VTLDEL


Total weight
15464.77 Da
Max. entity 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: 97.8 %, Completeness: 88.4 %, Completeness (bb): 84.4 % Detail

Polymer type: polypeptide(L)

Total1H13C15N
All88.4 % (1435 of 1624)93.7 % (799 of 853)80.0 % (508 of 635)94.1 % (128 of 136)
Backbone84.4 % (672 of 796)93.3 % (252 of 270)75.0 % (297 of 396)94.6 % (123 of 130)
Sidechain92.3 % (882 of 956)93.8 % (547 of 583)89.9 % (330 of 367)83.3 % (5 of 6)
Aromatic66.7 % (60 of 90)84.4 % (38 of 45)50.0 % (22 of 44) 0.0 % (0 of 1)
Methyl96.5 % (166 of 172)95.3 % (82 of 86)97.7 % (84 of 86)

1. RelE

GSHMAYFLDF DERALKEWRK LGSTVREQLK KKLVEVLESP RIEANKLRGM PDCYKIKLRS SGYRLVYQVI DEKVVVFVIS VGKAEASEVY SEAVKRIL

2. RelBc

GSHKQTLLSD EDAELVEIVK ERLRNPKPVR VTLDEL

Sample #1

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05), Details 13C,15N labeled RelE complexed with unlabeled RelBc.


#NameIsotope labelingTypeConcentration
1RelE[U-13C; U-15N]0.5 (±0.2) mM
2RelBcnatural abundance0.5 (±0.2) mM
3sodium phosphatenatural abundance25 mM
4sodium chloridenatural abundance500 mM
5DTTnatural abundance1 mM
6sodium azidenatural abundance0.5 mM
Sample #2

Solvent system 90% H2O/10% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05), Details 13C,15N labeled RelBc complexed with unlabeled RelE.


#NameIsotope labelingTypeConcentration
7RelEnatural abundance0.5 (±0.1) mM
8RelBc[U-13C; U-15N]0.5 (±0.1) mM
9sodium phosphatenatural abundance25 (±2.5) mM
10sodium chloridenatural abundance500 (±50.0) mM
11DTTnatural abundance1 (±0.1) mM
12sodium azidenatural abundance0.5 (±0.1) mM
Sample #3

Solvent system 100% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05), Details 13C,15N labeled RelE complexed with unlabeled RelBc.


#NameIsotope labelingTypeConcentration
13RelE[U-13C; U-15N]0.5 (±0.1) mM
14RelBcnatural abundance0.5 (±0.1) mM
15sodium phosphatenatural abundance25 (±2.5) mM
16sodium chloridenatural abundance500 (±50.0) mM
17DTTnatural abundance1 (±0.1) mM
18sodium azidenatural abundance0.5 (±0.1) mM
Sample #4

Solvent system 100% D2O, Pressure 1 atm, Temperature 296.5 (±0.1) K, pH 6.5 (±0.05), Details 13C,15N labeled RelBc complexed with unlabeled RelE.


#NameIsotope labelingTypeConcentration
19RelEnatural abundance0.5 (±0.1) mM
20RelBc[U-13C; U-15N]0.5 (±0.1) mM
21sodium phosphatenatural abundance25 (±2.5) mM
22sodium chloridenatural abundance500 (±50.0) mM
23DTTnatural abundance1 (±0.1) mM
24sodium azidenatural abundance0.5 (±0.1) mM

Protein Blocks Logo
Calculated from 20 models in PDB: 2KC8, Strand ID: A, B 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 ,
Related entities 1. RelE, : 1 : 1 : 7 : 5 entities Detail
Related entities 2. RelBc, : 1 : 3 : 4 entities Detail
Interaction partners 1. RelE, : 12 : 1 interactors Detail
Interaction partners 2. RelBc, : 1 : 1 interactors Detail
Experiments performed 24 experiments Detail
NMR combined restraints 5 contents Detail
Keywords antitoxin, mRNA interferase, RelB, RelE, toxin, translation inhibitor, antitoxin RelB, protein/protein complex, toxin RelE