BMRB Entry 30021

Title:
Solution structure of the pore-forming region of C. elegans Mitochondrial Calcium Uniporter (MCU)   PubMed: 27135929
Deposition date:
2016-02-23
Original release date:
2016-05-23
Authors:
Oxenoid, K.; Dong, Y.; Cao, C.; Cui, T.; Sancak, Y.; Markhard, A.; Grabarek, Z.; Kong, L.; Liu, Z.; Ouyang, B.; Cong, Y.; Mootha, V.; Chou, J.
Citation:

Citation: Oxenoid, K.; Dong, Y.; Cao, C.; Cui, T.; Sancak, Y.; Markhard, A.; Grabarek, Z.; Kong, L.; Liu, Z.; Ouyang, B.; Cong, Y.; Mootha, V.; Chou, J.. "Architecture of the Mitochondrial Calcium Uniporter"  Nature 533, 269-273 (2016).

Assembly members:

Assembly members:
Mitochondrial Calcium Uniporter, polymer, 159 residues, 18927.207 Da.

Natural source:

Natural source:   Common Name: nematodes   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

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

Experimental source:

Natural source:   Common Name: nematodes   Taxonomy ID: 6239   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Caenorhabditis elegans

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

Data sets:
Data typeCount
13C chemical shifts385
15N chemical shifts136
1H chemical shifts136

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity 11
2entity 21
3entity 31
4entity 41
5entity 51

Entities:

Entity 1, entity 1 159 residues - 18927.207 Da.

1   METALAALALEUSERVALASPGLUTYRLYS
2   LEUSERARGGLULYSLYSLEULEULEUGLN
3   LEUGLUASNALAGLUTHRLEULEUALAPRO
4   LEUHISASPALALYSARGLYSILEGLUGLN
5   GLUALAGLUALAHISTHRASPARGVALALA
6   TRPALAGLYPHEALAALASERGLYVALGLN
7   THRGLYLEUPHEALAARGLEUTHRTRPTRP
8   GLUTYRSERTRPASPILEVALGLUPROVAL
9   THRTYRPHEALATHRTYRSERTHRVALALA
10   ALATHRPHEGLYTYRTYRLEUTYRTHRGLN
11   GLNSERPHEGLUTYRPROSERALAARGGLU
12   ARGVALTYRTHRLYSGLNPHETYRARGARG
13   ALAGLNLYSGLNASNPHEASPILEGLULYS
14   TYRASNARGLEUVALTHRGLUVALASPGLU
15   LEUARGASNGLNLEULYSARGLEUARGASP
16   PROLEUGLUHISHISHISHISHISHIS

Samples:

sample_1: EDTA 2 ± 1 mM; Foscholine-14 27 ± 5 mM; MCU-dNTD, [100% 13C; 100% 15N; 85% 2H], 0.8 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_2: EDTA 2 ± 1 mM; Foscholine-14, [100% 2H at acyl chain], 27 ± 5 mM; MCU-dNTD, [100% 13C; 100% 15N], 0.8 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_3: EDTA 2 ± 1 mM; Foscholine-14, [100% 2H at acyl chain], 27 ± 5 mM; MCU-dNTD-1, [100% 15N; 100% 2H], 0.4 ± 0.05 mM; MCU-dNTD-2, [15% 13C], 0.4 ± 0.05 mM; MES 20 ± 1 mM; NaCl 75 ± 1 mM; NaN3 0.3 ± 0.5 mM; H2O 95%; D2O 5%

sample_conditions_1: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 306 K

sample_conditions_2: ionic strength: 100 mM; pH: 6.5; pressure: 1 atm; temperature: 306 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N TROSYsample_1isotropicsample_conditions_1
3D tr-HNCAsample_1isotropicsample_conditions_2
3D tr-HN(CO)CAsample_1isotropicsample_conditions_2
3D tr-HN(CA)COsample_1isotropicsample_conditions_2
3D tr-HNCOsample_1isotropicsample_conditions_2
3D tr-HN(CA)CBsample_1isotropicsample_conditions_2
3D 15N-15N HSQC-NOESY-TROSYsample_1isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_2isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_2isotropicsample_conditions_2
3D 1H-13C Methyl NOESYsample_2isotropicsample_conditions_1
3D 1H-13C Methyl NOESYsample_2isotropicsample_conditions_2
3D 1H-15N NOESY-TROSYsample_3isotropicsample_conditions_1
3D 1H-15N NOESY-TROSYsample_3isotropicsample_conditions_2
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_3isotropicsample_conditions_1

Software:

CcpNMR, CCPN - chemical shift assignment

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

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

TALOS, Cornilescu, Delaglio and Bax - data analysis

XEASY, Bartels et al. - chemical shift assignment

XPLOR-NIH, Schwieters et al - structure calculation

NMR spectrometers:

  • Bruker AvanceII 600 MHz
  • Bruker AvanceIII 900 MHz

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