BMRB Entry 17541

Title:
Structure of the first domain of human Smurf1 in complex with a monophosphorylated human Smad1 derived peptide.
Deposition date:
2011-03-22
Original release date:
2011-06-23
Authors:
Macias, Maria; Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan
Citation:

Citation: Aragon, Eric; Goerner, Nina; Zaromytidou, Alexia-Ileana; Xi, Qiaoran; Escobedo, Albert; Massague, Joan; Macias, Maria. "A Smad action turnover switch operated by WW domain readers of a phosphoserine code."  Genes Dev. 25, 1275-1288 (2011).
PubMed: 21685363

Assembly members:

Assembly members:
human Smurf1, polymer, 33 residues, 3878.262 Da.
phosphorylated human Smad1 derived peptide, polymer, 8 residues, 913.831 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: pETM11

Entity Sequences (FASTA):

Entity Sequences (FASTA):
human Smurf1: ELPEGYEQRTTVQGQVYFLH TQTGVSTWHDPRI
phosphorylated human Smad1 derived peptide: SDPGXPFQ

Data sets:
Data typeCount
1H chemical shifts224

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1human Smurf11
2phosphorylated human Smad1 derived peptide2

Entities:

Entity 1, human Smurf1 33 residues - 3878.262 Da.

1   GLULEUPROGLUGLYTYRGLUGLNARGTHR
2   THRVALGLNGLYGLNVALTYRPHELEUHIS
3   THRGLNTHRGLYVALSERTHRTRPHISASP
4   PROARGILE

Entity 2, phosphorylated human Smad1 derived peptide 8 residues - 913.831 Da.

1   SERASPPROGLYSEPPROPHEGLN

Samples:

H: NEDD4LWW3 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N: NEDD4LWW3, [U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

15N13C: NEDD4LWW3, [U-100% 13C; U-100% 15N], 1 mM; SMAD3 3 mM; sodium phosphate 20 mM; sodium chloride 100 mM; sodium azide 2 mM; H2O 90%; D2O 10%

sample_conditions_1: ionic strength: 0.420 M; pH: 7; pressure: 1 atm; temperature: 285 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYHisotropicsample_conditions_1
2D 1H-1H TOCSYHisotropicsample_conditions_1
3D CBCA(CO)NH15N13Cisotropicsample_conditions_1
3D HNCACB15N13Cisotropicsample_conditions_1
2D 1H-15N HSQC15Nisotropicsample_conditions_1

Software:

CNS v1.3, Brunger, Adams, Clore, Gros, Nilges and Read - structure solution

XEASY, Bartels et al. - chemical shift assignment

TOPSPIN, Bruker Biospin - collection

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

NMR spectrometers:

  • Bruker DRX 600 MHz

Related Database Links:

BMRB 17542
PDB
DBJ BAB13451 BAB29770 BAE32623 BAG11347
GB AAC62434 AAD52564 AAF08298 AAH29097 AAH59201
REF NP_001001943 NP_001033716 NP_001081939 NP_001103068 NP_001186776
SP Q9CUN6 Q9HCE7 Q9PUN2
TPG DAA15146
AlphaFold Q9UFT8 Q9PUN2 Q9CUN6 Q9HCE7