BMRB Entry 34115

Title:
Solution structure of detergent-solubilized Rcf1, a yeast mitochondrial inner membrane protein involved in respiratory Complex III/IV supercomplex formation   PubMed: 29507228
Deposition date:
2017-03-13
Original release date:
2018-02-23
Authors:
Zhou, S.; Pettersson, P.; Sjoholm, J.; Sjostrand, D.; Hogbom, M.; Brzezinski, P.; Maler, L.; Adelroth, P.
Citation:

Citation: Zhou, Shu; Pettersson, Pontus; Huang, Jingjing; Sjoholm, Johannes; Sjostrand, Dan; Pomes, Regis; Hogbom, Martin; Brzezinski, Peter; Maler, Lena; Adelroth, Pia. "Solution NMR structure of yeast Rcf1, a protein involved in respiratory supercomplex formation."  Proc. Natl. Acad. Sci. U.S.A. 115, 3048-3053 (2018).

Assembly members:

Assembly members:
entity_1, polymer, 174 residues, 20388.496 Da.

Natural source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Experimental source:

Natural source:   Common Name: Baker's yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli K-12

Data sets:
Data typeCount
13C chemical shifts623
15N chemical shifts149
1H chemical shifts1007

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_1, 11
2entity_1, 21

Entities:

Entity 1, entity_1, 1 174 residues - 20388.496 Da.

1   METSERARGMETPROSERSERPHEASPVAL
2   THRGLUARGASPLEUASPASPMETTHRPHE
3   GLYGLUARGILEILETYRHISCYSLYSLYS
4   GLNPROLEUVALPROILEGLYCYSLEULEU
5   THRTHRGLYALAVALILELEUALAALAGLN
6   ASNVALARGLEUGLYASNLYSTRPLYSALA
7   GLNTYRTYRPHEARGTRPARGVALGLYLEU
8   GLNALAALATHRLEUVALALALEUVALALA
9   GLYSERPHEILETYRGLYTHRSERGLYLYS
10   GLULEULYSALALYSGLUGLUGLNLEULYS
11   GLULYSALALYSMETARGGLULYSLEUTRP
12   ILEGLNGLULEUGLUARGARGGLUGLUGLU
13   THRGLUALAARGARGLYSARGALAGLULEU
14   ALAARGMETLYSTHRLEUGLUASNGLUGLU
15   GLUILELYSASNLEUGLULYSGLULEUSER
16   ASPLEUGLUASNLYSLEUGLYLYSLYSGLU
17   PHEARGVALPROGLYSERHISHISHISHIS
18   HISHISHISHIS

Samples:

sample_2: rcf1, [U-13C; U-15N; U-2H], 0.4 mM

sample_3: rcf1, [U-13C; U-15N], 0.4 mM

sample_4: rcf1, [U-13C; U-15N; 50% U-2H], 0.4 mM

sample_5: rcf1, [U-15N; U-2H; 99%-1HD, 13CD-IL; 99%-1HG, 13CG-V], 0.4 mM

sample_6: rcf1, [U-50% 13C; U-50% 15N; U-50% 12C; U-50% 14N], 0.4 mM

sample_1: rcf1, [U-15N], 0.4 mM

sample_conditions_1: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_2: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_3: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_4: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_5: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

sample_conditions_6: ionic strength: 0 mM; pH: 5.0; pressure: 1 Pa; temperature: 323 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_2
3D HN(COCA)CBsample_2isotropicsample_conditions_2
3D HNCOsample_2isotropicsample_conditions_2
3D HN(CA)COsample_2isotropicsample_conditions_2
3D HNCAsample_2isotropicsample_conditions_2
3D HN(CO)CAsample_2isotropicsample_conditions_2
3D N-NOESY-HSQCsample_2isotropicsample_conditions_2
3D HCCH-TOCSYsample_3isotropicsample_conditions_3
3D CC(CO)NHsample_3isotropicsample_conditions_3
3D H(CCO)NHsample_3isotropicsample_conditions_3
2D 1H-13C HSQCsample_3isotropicsample_conditions_3
3D N-NOESY-HSQCsample_3isotropicsample_conditions_3
3D C-NOESY-HSQCsample_3isotropicsample_conditions_3
2D 1H-13C HSQCsample_4isotropicsample_conditions_4
3D N-NOESY-HSQCsample_4isotropicsample_conditions_4
3D C-NOESY-HSQCsample_4isotropicsample_conditions_4
2D 1H-13C HSQCsample_5isotropicsample_conditions_5
3D C-NOESY-HSQCsample_5isotropicsample_conditions_5
3D F1-13C/15N-filtered, F3-15N-edited-NOESY-HSQCsample_6isotropicsample_conditions_6
3D F1-13C/15N-filtered, F3-13C-edited-NOESY-HSQCsample_6isotropicsample_conditions_6

Software:

TOPSPIN, Bruker Biospin - collection

CcpNMR, CCPN - chemical shift assignment

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - structure calculation

NMR spectrometers:

  • Bruker AvanceIII 900 MHz
  • Bruker AvanceIII 700 MHz

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