BMRB Entry 15753

Title:
Structure of a Glycosylphosphatidylinositol-anchored Domain from a Trypanosome Variant Surface Glycoprotein
Deposition date:
2008-05-05
Original release date:
2008-11-12
Authors:
Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark
Citation:

Citation: Jones, Nicola; Nietlispach, Daniel; Sharma, Reuben; Burke, David; Eyres, Isobel; Mues, Marsilius; Mott, Helen; Carrington, Mark. "Structure of a glycosylphosphatidylinositol-anchored domain from a trypanosome variant surface glycoprotein"  J. Biol. Chem. 283, 3584-3593 (2008).
PubMed: 18003615

Assembly members:

Assembly members:
Variant_Surface_Glycoprotein_ILTat1.24, polymer, 46 residues, 5141.820 Da.

Natural source:

Natural source:   Common Name: not available   Taxonomy ID: 5691   Superkingdom: Eukaryota   Kingdom: not available   Genus/species: Trypanosoma brucei

Experimental source:

Experimental source:   Production method: recombinant technology   Host organism: Escherichia coli   Vector: pET15b

Entity Sequences (FASTA):

Entity Sequences (FASTA):
Variant_Surface_Glycoprotein_ILTat1.24: GKSPEAECNKITEEPKCSEE KICSWHKEVKAGEKNCQFNS TKASKS

Data sets:
Data typeCount
1H chemical shifts298

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1entity1

Entities:

Entity 1, entity 46 residues - 5141.820 Da.

This is the first C-terminal subdomain of the Variant Surface Glycoprotein ILTat1.24

1   GLYLYSSERPROGLUALAGLUCYSASNLYS
2   ILETHRGLUGLUPROLYSCYSSERGLUGLU
3   LYSILECYSSERTRPHISLYSGLUVALLYS
4   ALAGLYGLULYSASNCYSGLNPHEASNSER
5   THRLYSALASERLYSSER

Samples:

sample_1: ILTat1.24 C1-domain 0.5 mM; sodium phosphate 50 mM; sodium chloride 150 mM; sodium azide 0.05%; D2O 10%; H2O 90%

sample_conditions_1: pH: 6.0; pressure: 1 atm; temperature: 298 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-1H NOESYsample_1isotropicsample_conditions_1

Software:

AZARA, Boucher - processing

ANSIG, Kraulis - data analysis

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

NMR spectrometers:

  • Bruker DRX 800 MHz

Related Database Links:

PDB
EMBL CAA40086
GB AGH61239
SP P26329
AlphaFold P26329