BMRB Entry 11426

Title:
Solution structure of SecDF periplasmic domain P4
Deposition date:
2011-01-30
Original release date:
2012-01-30
Authors:
Tanaka, Takeshi; Tsukazaki, Tomoya; Echizen, Yuka; Nureki, Osamu; Kohno, Toshiyuki
Citation:

Citation: Tsukazaki, Tomoya; Mori, Hiroyuki; Echizen, Yuka; Ishitani, Ryuichiro; Fukai, Shuya; Tanaka, Takeshi; Perederina, Anna; Vassylyev, Dmitry; Kohno, Toshiyuki; Maturana, Andres; Ito, Koreaki; Nureki, Osamu. "Structure and function of a membrane component SecDF that enhances protein export"  Nature 474, 235-238 (2011).
PubMed: 21562494

Assembly members:

Assembly members:
entity, polymer, 92 residues, 10291.784 Da.

Natural source:

Natural source:   Common Name: bacteria   Taxonomy ID: 300852   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Thermus thermophilus

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pYE79

Data sets:
Data typeCount
13C chemical shifts380
15N chemical shifts96
1H chemical shifts610

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1periplasmic domain P4, residues 470-5591

Entities:

Entity 1, periplasmic domain P4, residues 470-559 92 residues - 10291.784 Da.

1   METVALGLYPHEASNTYRSERILEASPPHE
2   THRGLYGLYTHRALATYRTHRLEUARGALA
3   GLUPROASNVALGLUVALGLUTHRLEUARG
4   ARGPHELEUGLUGLULYSGLYPHEPROGLY
5   LYSGLUALAVALILETHRGLNVALGLNALA
6   PROTHRALAALATYRARGGLUPHELEUVAL
7   LYSLEUPROPROLEUSERASPGLUARGARG
8   LEUGLULEUGLUARGLEUPHEALASERGLU
9   LEULYSALATHRVALLEUALASERGLUTHR
10   VALGLY

Samples:

sample_1: P4 domain, [U-13C; U-15N], 1 mM; TRIS 20 mM; sodium chloride 50 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 50 mM; pH: 6.5; pressure: 1 atm; temperature: 303 K

Experiments:

NameSampleSample stateSample conditions
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

TALOS, Cornilescu, Delaglio and Bax - structure solution

ProcheckNMR, Laskowski and MacArthur - structure solution

NMR spectrometers:

  • Bruker Avance 500 MHz

Related Database Links:

PDB
DBJ BAD70520
GB AAS80693
REF WP_011172795 YP_143963
SP Q5SKE6
AlphaFold Q5SKE6

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