BMRB Entry 16926

Title:
NMR Structure of Escherichia coli BamE, a Lipoprotein Component of the beta-Barrel Assembly Machinery Complex   PubMed: 21207987
Deposition date:
2010-05-13
Original release date:
2011-01-06
Authors:
Kim, Kelly; Okon, Mark; Escobar, Eric; Kang, Hyun-Seo; McIntosh, Lawrence; Paetzel, Mark
Citation:

Citation: Kim, Kelly; Kang, Hyun-Seo; Okon, Mark; Escobar-Cabrera, Eric; McIntosh, Lawrence; Paetzel, Mark. "Structural Characterization of Escherichia coli BamE, a Lipoprotein Component of the -Barrel Assembly Machinery Complex."  Biochemistry 50, 1081-1090 (2011).

Assembly members:

Assembly members:
E._coli_lipoprotein, polymer, 97 residues, 8072.073 Da.

Natural source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Experimental source:

Natural source:   Common Name: E. coli   Taxonomy ID: 562   Superkingdom: Eubacteria   Kingdom: not available   Genus/species: Escherichia coli

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET28a

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts236
15N chemical shifts92
1H chemical shifts544

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1E. coli lipoprotein1

Entities:

Entity 1, E. coli lipoprotein 97 residues - 8072.073 Da.

First four residues (GSHM) are remainder of thrombin-cleaved 6-His tag. This structure represents the full length mature BamE protein without its lipidated cysteine (Cys20).

1   GLYSERHISMETSERTHRLEUGLUARGVAL
2   VALTYRARGPROASPILEASNGLNGLYASN
3   TYRLEUTHRALAASNASPVALSERLYSILE
4   ARGVALGLYMETTHRGLNGLNGLNVALALA
5   TYRALALEUGLYTHRPROLEUMETSERASP
6   PROPHEGLYTHRASNTHRTRPPHETYRVAL
7   PHEARGGLNGLNPROGLYHISGLUGLYVAL
8   THRGLNGLNTHRLEUTHRLEUTHRPHEASN
9   SERSERGLYVALLEUTHRASNILEASPASN
10   LYSPROALALEUSERGLYASN

Samples:

sample_1: E. coli protein, [U-100% 13C; U-100% 15N], 0.5 mM; D2O 15%; H2O 85%; Na2HPO4/NaH2PO4 20 mM

Phosphate_Buffer: ionic strength: 0.02 M; pH: 6.6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicPhosphate_Buffer
3D CBCA(CO)NHsample_1isotropicPhosphate_Buffer
3D 1H-15N NOESYsample_1isotropicPhosphate_Buffer
3D HNCOsample_1isotropicPhosphate_Buffer
3D HNCACBsample_1isotropicPhosphate_Buffer
3D HN(CO)CAsample_1isotropicPhosphate_Buffer
3D 1H-13C NOESYsample_1isotropicPhosphate_Buffer
2D 1H-1H COSYsample_1isotropicPhosphate_Buffer

Software:

SPARKY v3.113, Goddard - chemical shift assignment, peak picking

CYANA v2.1, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Varian Unity 500 MHz

Related Database Links:

BMRB 16424
PDB
DBJ BAA16502 BAB36902 BAG78424 BAI26856 BAI31942
EMBL CAH23267 CAP77059 CAQ32986 CAQ88015 CAQ99565
GB AAA79787 AAC75666 AAG57727 AAN44171 AAN81589
REF NP_311506 NP_417107 NP_708464 WP_001203434 WP_001203436
SP P0A937 P0A938 P0A939 Q32CX2
AlphaFold P0A938

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts