BMRB Entry 17727

Title:
3D ssNMR structure of membrane embedded KcsA-Kv1.3 channel (Closed state)
Deposition date:
2011-08-11
Original release date:
2012-06-21
Authors:
Nand, D.; Ader, C.; Prokofyev, A.; Hornig, S.; A Bonvin, M.; Killian, A.; Becker, S.; Pongs, O.; Baldus, M.
Citation:

Citation: van der Cruijsen, Elwin; Nand, Deepak; Weingarth, Markus; Prokofyev, Alexander; Hornig, Sonke; Cukkemane, Abhishek Arun; Bonvin, Alexandre M J J; Becker, Stefan; Hulse, Raymond; Perozo, Eduardo; Pongs, Olaf; Baldus, Marc. "Importance of lipid-pore loop interface for potassium channel structure and function."  Proc. Natl. Acad. Sci. U.S.A. 110, 13008-13013 (2013).
PubMed: 23882077

Assembly members:

Assembly members:
KcsA-Kv1.3_(Closed_state), polymer, 94 residues, 9775.335 Da.

Natural source:

Natural source:   Common Name: Streptomyces lividans   Taxonomy ID: 1916   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Streptomyces lividans

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pQE32

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts270
15N chemical shifts41

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1KcsA-Kv1.3 (Closed state)_11
2KcsA-Kv1.3 (Closed state)_21
3KcsA-Kv1.3 (Closed state)_31
4KcsA-Kv1.3 (Closed state)_41

Entities:

Entity 1, KcsA-Kv1.3 (Closed state)_1 94 residues - 9775.335 Da.

1   SERALALEUHISTRPARGALAALAGLYALA
2   ALATHRVALLEULEUVALILEVALLEULEU
3   ALAGLYSERTYRLEUALAVALLEUALAGLU
4   ALAASPASPPROTHRSERGLYPHESERSER
5   ILEPROASPALALEUTRPTRPSERVALGLU
6   THRALATHRTHRVALGLYTYRGLYASPLEU
7   TYRPROVALTHRLEUTRPGLYARGCYSVAL
8   ALAVALVALVALMETVALALAGLYILETHR
9   SERPHEGLYLEUVALTHRALAALALEUALA
10   THRTRPPHEVAL

Samples:

sample_1: KcsA-Kv1.3 (Closed state), [U-100% 13C; U-100% 15N], 50 mM; potassium ions 50 mM; H2O 100%

sample_2: KcsA-Kv1.3 (Closed state), [U-100% 13C; U-100% 15N; U-80% 2H], 5 mM; H2O 100%

sample_conditions_1: pH: 7.4; temperature: 243 K

Experiments:

NameSampleSample stateSample conditions
2D_13C-13C_CHHCsample_1solidsample_conditions_1
2D_13C-13C_Proton driven spin difussionsample_2solidsample_conditions_1

Software:

CNS_HADDOCK, Brunger, Adams, Clore, Gros, Nilges and Read, (HADDOCK) - structure solution(Monomer)

NMR spectrometers:

  • Bruker Avance 600, 800 MHz
  • Bruker AvanceIII 700 MHz

Related Database Links:

BMRB 17744