BMRB Entry 19622

Title:
Solution structure of oxidized [2Fe-2S] ferredoxin PetF from Chlamydomonas reinhardtii
Deposition date:
2013-11-19
Original release date:
2014-11-17
Authors:
Rumpel, Sigrun; Siebel, Judith; Fares, Christophe; Reijerse, Edward; Lubitz, Wolfgang
Citation:

Citation: Rumpel, Sigrun; Siebel, Judith; Fares, Christophe; Happe, Thomas; Lubitz, Wolfgang; Reijerse, Edward; Winkler, Martin. "Redirecting Elctrons from Photosystem I to Hydrogenase: Towards Increased Hydrogen Production in Algae"  Biochemistry ., .-..

Assembly members:

Assembly members:
entity_1, polymer, 101 residues, 10840.030 Da.
FE2/S2 (INORGANIC) CLUSTER, non-polymer, 175.820 Da.

Natural source:

Natural source:   Common Name: Green Algae   Taxonomy ID: 3055   Superkingdom: Eukaryota   Kingdom: Viridiplantae   Genus/species: Chlamydomonas reinhardtii

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET21b

Data sets:
Data typeCount
13C chemical shifts371
15N chemical shifts88
1H chemical shifts575

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1PetF monomer1
2FE2/S2 (INORGANIC) CLUSTER2

Entities:

Entity 1, PetF monomer 101 residues - 10840.030 Da.

1   METTYRLYSVALTHRLEULYSTHRPROSER
2   GLYASPLYSTHRILEGLUCYSPROALAASP
3   THRTYRILELEUASPALAALAGLUGLUALA
4   GLYLEUASPLEUPROTYRSERCYSARGALA
5   GLYALACYSSERSERCYSALAGLYLYSVAL
6   ALAALAGLYTHRVALASPGLNSERASPGLN
7   SERPHELEUASPASPALAGLNMETGLYASN
8   GLYPHEVALLEUTHRCYSVALALATYRPRO
9   THRSERASPCYSTHRILEGLNTHRHISGLN
10   GLUGLUALALEUTYRGLUASNLEUTYRPHE
11   GLN

Entity 2, FE2/S2 (INORGANIC) CLUSTER - Fe2 S2 - 175.820 Da.

1   FES

Samples:

sample_1: PetF monomer mM; potassium phosphate 50 mM; sodium chloride 50 mM; DTT 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.1 M; pH: 6.8; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
3D C(CO)NHsample_1isotropicsample_conditions_1
3D H(CCO)NHsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1

Software:

ARIA, Linge, O'Donoghue and Nilges - structure solution

CNS, Brunger, Adams, Clore, Gros, Nilges and Read - refinement

SPARKY, Goddard - data analysis

ProcheckNMR, Laskowski and MacArthur - data analysis

TOPSPIN, Bruker Biospin - collection

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

PDB
GB AAA33085 AAC49171 ABA01123 EDP03827
REF XP_001692808
SP P07839
AlphaFold P07839

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