BMRB Entry 17765

Title:
Identification of the key regions that drive functional amyloid formation by the fungal hydrophobin EAS
Deposition date:
2011-07-06
Original release date:
2012-01-24
Authors:
Macindoe, Ingrid; Kwan, Ann; Morris, Vanessa; Mackay, Joel; Sunde, Margie
Citation:

Citation: Macindoe, Ingrid; Kwan, Ann; Ren, Qin; Morris, Vanessa; Yang, Wenrong; Mackay, Joel; Sunde, Margaret. "Self-assembly of functional, amphipathic amyloid monolayers by the fungal hydrophobin EAS."  Proc. Natl. Acad. Sci. U.S.A. 109, E804-E811 (2012).
PubMed: 22308366

Assembly members:

Assembly members:
entity, polymer, 68 residues, 6728.595 Da.

Natural source:

Natural source:   Common Name: Neurospora crassa   Taxonomy ID: 5141   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Neurospora crassa

Experimental source:

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

Entity Sequences (FASTA):

Data sets:
Data typeCount
1H chemical shifts420

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1EAS1

Entities:

Entity 1, EAS 68 residues - 6728.595 Da.

Residue 1 represents a cloning artifact.

1   SERALATHRTHRILEGLYPROASNTHRCYS
2   SERILEASPASPTYRLYSPROTYRCYSCYS
3   GLNSERMETSERGLYSERALASERLEUGLY
4   CYSVALVALGLYVALILEGLYSERGLNCYS
5   GLYALASERVALLYSCYSCYSLYSASPASP
6   VALTHRASNTHRGLYASNSERGLYLEUILE
7   ILEASNALAALAASNCYSVALALA

Samples:

sample_1: EAS 890 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM

sample_2: EAS, [U-98% 15N], 280 uM; D2O 5%; H2O 95%; DSS20 – 34 uM; sodium phosphate 20 mM

sample_conditions_1: ionic strength: 20 mM; pH: 7; pressure: 1 atm; temperature: 298 K

sample_conditions_2: ionic strength: 20 mM; pH: 6; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D DQF-COSYsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_1isotropicsample_conditions_1
2D 1H-1H NOESYsample_1isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_2
3D HNHAsample_2isotropicsample_conditions_2

Software:

TOPSPIN vv1.3, Bruker Biospin - collection, processing

SPARKY, Goddard - chemical shift assignment, data analysis, peak picking

ARIA vv1.2, Linge, O'Donoghue and Nilges - refinement, structure solution

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

ProcheckNMR, Laskowski and MacArthur - structure validation

Molmol, Koradi, Billeter and Wuthrich - data analysis

NMR spectrometers:

  • Bruker Avance 600 MHz

Related Database Links:

BMRB 15863
PDB