BMRB Entry 26592

Title:
The LcrG tip chaperone protein of the Yersinia pestis type III secretion system is partially folded
Deposition date:
2015-06-22
Original release date:
2015-12-18
Authors:
De Guzman, Roberto; Chaudhury, Sukanya
Citation:

Citation: Chaudhury, Sukanya; Souza, Clarice; Plano, Gregory; De Guzman, Roberto. "The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded"  J. Mol. Biol. 427, 3096-3109 (2015).
PubMed: 26259880

Assembly members:

Assembly members:
LcrG, polymer, 67 residues, Formula weight is not available

Natural source:

Natural source:   Common Name: enterobacteria   Taxonomy ID: 632   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Yersinia pestis

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET-21a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts163
15N chemical shifts78
1H chemical shifts78

Additional metadata:

  • Assembly
  • Samples and Experiments
  • Software
  • Spectrometers
  • Hide all

Assembly:

Entity Assembly IDEntity NameEntity ID
1LcrG 7-731

Entities:

Entity 1, LcrG 7-73 67 residues - Formula weight is not available

The sequence corresponds to LcrG residues 7-73

1   ASPGLUTYRASPLYSTHRLEULYSGLNALA
2   GLULEUALAILEALAASPSERASPHISARG
3   ALALYSLEULEUGLNGLUMETSERALAASP
4   ILEGLYLEUTHRPROGLUALAVALMETLYS
5   ILEPHEALAGLYARGSERALAGLUGLUILE
6   LYSPROALAGLUARGGLULEULEUASPGLU
7   ILELYSARGGLNARGGLUARG

Samples:

sample_1: LcrG, [U-99% 13C; U-99% 15N], 0.9 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%

sample_2: LcrG in complex with LcrV, U-99% 13C; U-99% 15N], 0.6 mM; sodium phosphate mM; sodium chloride mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 10 mM; pH: 7.0; pressure: 1 atm; temperature: 273 K

sample_conditions_2: ionic strength: 10 mM; pH: 7.0; temperature: 273 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HNCACBsample_2isotropicsample_conditions_2

Software:

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - processing

NMRView, Johnson, One Moon Scientific - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 800 MHz

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks