BMRB

Biological Magnetic Resonance Data Bank


A Repository for Data from NMR Spectroscopy on Proteins, Peptides, Nucleic Acids, and other Biomolecules
Member of WWPDB

BMRB Entry 18445

Title: NMR high resolution structures of free Tah1 and Tah1 bound to the Hsp90 C-terminal tail explain how Hsp90 recognizes the R2TP complex   PubMed: 24012479

Authors: BACK, Regis; DOMINGUEZ, Cyril; ROTHE, Benjamin; BOBO, Claude; BEAUFILS, Chrystel; MORERA, Solange; MEYER, Philippe; CHARPENTIER, Bruno; BRANLANT, Christiane; ALLAIN, Frederic H.-T.; MANIVAL, Xavier

Citation: Back, Regis; Dominguez, Cyril; Rothe, Benjamin; Bobo, Claude; Beaufils, Chrystel; Morera, Solange; Meyer, Philippe; Charpentier, Bruno; Branlant, Christiane; Allain, Frederic H-T; Manival, Xavier. "High-resolution structural analysis shows how Tah1 tethers Hsp90 to the R2TP complex."  Structure 21, 1834-1847 (2013).

Assembly members:
entity, polymer, 110 residues, 12393.052 Da.

Natural source:   Common Name: bakers yeast   Taxonomy ID: 4932   Superkingdom: Eukaryota   Kingdom: Fungi   Genus/species: Saccharomyces cerevisiae

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

Entity Sequences (FASTA):
entity: SQFEKQKEQGNSLFKQGLYR EAVHCYDQLITAQPQNPVGY SNKAMALIKLGEYTQAIQMC QQGLRYTSTAEHVAIRSKLQ YRLELAQGAVGSVQIPVVEV DELPEGYDRS

Data sets:
Data typeCount
13C chemical shifts327
1H chemical shifts760

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1yeast Tah11

Entities:

Entity 1, yeast Tah1 110 residues - 12393.052 Da.

1   SERGLNPHEGLULYSGLNLYSGLUGLNGLY
2   ASNSERLEUPHELYSGLNGLYLEUTYRARG
3   GLUALAVALHISCYSTYRASPGLNLEUILE
4   THRALAGLNPROGLNASNPROVALGLYTYR
5   SERASNLYSALAMETALALEUILELYSLEU
6   GLYGLUTYRTHRGLNALAILEGLNMETCYS
7   GLNGLNGLYLEUARGTYRTHRSERTHRALA
8   GLUHISVALALAILEARGSERLYSLEUGLN
9   TYRARGLEUGLULEUALAGLNGLYALAVAL
10   GLYSERVALGLNILEPROVALVALGLUVAL
11   ASPGLULEUPROGLUGLYTYRASPARGSER

Samples:

sample_1: Tah1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 150 mM; H2O 90%; D2O 10%

sample_2: Tah1, [U-100% 13C; U-100% 15N], 1 mM; sodium phosphate 10 mM; sodium chloride 150 mM; D2O 150 mM

sample_conditions_1: ionic strength: 160 mM; pH: 7.2; pressure: 1 atm; temperature: 288 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
3D HNCOsample_1isotropicsample_conditions_1
3D HNCACBsample_1isotropicsample_conditions_1
3D CBCA(CO)NHsample_1isotropicsample_conditions_1
3D HNCAsample_1isotropicsample_conditions_1
3D HNHAsample_1isotropicsample_conditions_1
3D HCCH-TOCSYsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_1isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aliphaticsample_1isotropicsample_conditions_1
3D 1H-13C NOESY aromaticsample_1isotropicsample_conditions_1
2D 1H-1H TOCSYsample_2isotropicsample_conditions_1
2D 1H-1H NOESYsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1

Software:

TOPSPIN, Bruker Biospin - collection

SPARKY, Goddard - chemical shift assignment

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

CYANA, Guntert, Mumenthaler and Wuthrich - structure solution

NMR spectrometers:

  • Bruker Avance 600 MHz
  • Bruker Avance 750 MHz

Related Database Links:

BMRB 17312 18447
PDB
DBJ GAA21965
EMBL CAA42288 CAY78265
GB AAS56477 AHN96120 AHV79323 AHY79733 AJP37484
REF NP_009986
SP P25638
TPG DAA07534