BMRB Entry 34726

Title:
RNA binding induces an allosteric switch in Cyp33 to repress MLL1 mediated transcription regulation
Deposition date:
2022-03-31
Original release date:
2022-04-11
Authors:
Blatter, M.; Allain, F.; Meylan, C.
Citation:

Citation: Blatter, Markus; Meylan, Charlotte; Clery, Antoine; Giambruno, Roberto; Nikolaev, Yaroslav; Heidecker, Michel; Solanki, Jessica Arvindbhai; Diaz, Manuel; Gabellini, Davide; Allain, Frederic H-T. "RNA binding induces an allosteric switch in Cyp33 to repress MLL1-mediated transcription"  Sci. Adv. 9, eadf5330-eadf5330 (2023).
PubMed: 37075125

Assembly members:

Assembly members:
entity_1, polymer, 93 residues, 10349.721 Da.
entity_2, polymer, 8 residues, 2527.545 Da.

Natural source:

Natural source:   Common Name: Human   Taxonomy ID: 9606   Superkingdom: Eukaryota   Kingdom: Metazoa   Genus/species: Homo sapiens

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: PTYB12

Entity Sequences (FASTA):

Data sets:
Data typeCount
13C chemical shifts368
15N chemical shifts91
1H chemical shifts722

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1unit_11
2unit_22

Entities:

Entity 1, unit_1 93 residues - 10349.721 Da.

1   ALAGLYHISMETALATHRTHRLYSARGVAL
2   LEUTYRVALGLYGLYLEUALAGLUGLUVAL
3   ASPASPLYSVALLEUHISALAALAPHEILE
4   PROPHEGLYASPILETHRASPILEGLNILE
5   PROLEUASPTYRGLUTHRGLULYSHISARG
6   GLYPHEALAPHEVALGLUPHEGLULEUALA
7   GLUASPALAALAALAALAILEASPASNMET
8   ASNGLUSERGLULEUPHEGLYARGTHRILE
9   ARGVALASNLEUALALYSPROMETARGILE
10   LYSGLUGLY

Entity 2, unit_2 8 residues - 2527.545 Da.

1   UAAUGUCG

Samples:

sample_1: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 15N], 1 mM; RNA (5'-R(*UP*AP*AP*UP*GP*UP*CP*G)-3') 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM

sample_2: PEPTIDYL-PROLYL CIS-TRANS ISOMERASE E, [U-100% 13C; U-100% 15N], 1 mM; RNA (5'-R(*UP*AP*AP*UP*GP*UP*CP*G)-3') 1 mM; sodium chloride 40 mM; sodium phosphate 40 mM

sample_conditions_1: ionic strength: 80 mM; pH: 7; pressure: 1 atm; temperature: 310.15 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_2isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_2isotropicsample_conditions_1
3D F3-FILTERED- F2-EDITED 13C NOESYsample_2isotropicsample_conditions_1
2D 1H-13C HSQC aromaticsample_1isotropicsample_conditions_1
2D 1H-13C HSQC aliphaticsample_1isotropicsample_conditions_1
2D F2- FILTERED NOESYsample_2isotropicsample_conditions_1

Software:

Amber v10, Case, Darden, Cheatham III, Simmerling, Wang, Duke, Luo, ... and Kollman - refinement

CYANA, Guntert, Mumenthaler and Wuthrich - structure calculation

Sparky, Goddard - chemical shift assignment, peak picking

NMR spectrometers:

  • Bruker AVANCE III 900 MHz
  • Bruker AVANCE III 700 MHz

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