BMRB Entry 30559

Title:
Solution structure of the Tudor domain of PSHCP   PubMed: 31391250
Deposition date:
2019-01-14
Original release date:
2019-08-16
Authors:
Bauer, Katherine; Pelligrini, M.; Ragusa, Michael
Citation:

Citation: Bauer, Katherine; Dicovitsky, R.; Pellegrini, M.; Zhaxybayeva, O.; Ragusa, Michael. "The structure of a highly-conserved picocyanobacterial protein reveals a Tudor domain with an RNA-binding function"  J. Biol. Chem. 294, 14333-14344 (2019).

Assembly members:

Assembly members:
PSHCP, polymer, 59 residues, 6471.392 Da.

Natural source:

Natural source:   Common Name: Prochlorococcus marinus (strain MIT 9303)   Taxonomy ID: 59922   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Prochlorococcus Prochlorococcus marinus

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

Experimental source:

Natural source:   Common Name: Prochlorococcus marinus (strain MIT 9303)   Taxonomy ID: 59922   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Prochlorococcus Prochlorococcus marinus

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts247
15N chemical shifts61
1H chemical shifts409

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity_11

Entities:

Entity 1, entity_1 59 residues - 6471.392 Da.

1   SERASNALAMETGLULEUASPLEUGLNPRO
2   GLYASPVALVALLYSVALLEUGLUSERALA
3   ALALEUGLYTRPVALARGALAARGVALILE
4   ARGVALLYSSERGLYGLYARGVALVALVAL
5   GLNSERASPGLNGLYARGGLUPHETHRALA
6   ARGGLYASNGLNVALARGLEUILEGLU

Samples:

sample_1: PSHCP, [U-15N], 1.4 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM

sample_2: PSHCP, [U-15N, -13C], 1.6 mM; sodium phosphate 20 mM; sodium chloride 200 mM; TCEP 0.2 mM

sample_conditions_1: ionic strength: 200 mM; pH: 6.5; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
3D_15N-separated_NOESYsample_1isotropicsample_conditions_1
3D_13C-separated_NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HN(CO)CAsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_2isotropicsample_conditions_1
3D HN(CA)COsample_2isotropicsample_conditions_1
3D H(CCO)NHsample_2isotropicsample_conditions_1
2D_NOESYsample_1isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - processing

CNS, Brunger A. T. et.al. - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

CARA, Keller and Wuthrich - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker Avance 700 MHz

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