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 16270

Title: SOLUTION STRUCTURE OF THE S. AUREUS SORTASE A-SUBSTRATE COMPLEX   PubMed: 19592495

Deposition date: 2009-05-01 Original release date: 2009-07-16

Authors: Suree, Nuttee; Liew, Chu; Villareal, Valerie; Thieu, William; Fadeev, Evgeny; Clemens, Jeremy; Jung, Michael; Clubb, Robert

Citation: Suree, Nuttee; Liew, Chu; Villareal, Valerie; Thieu, William; Fadeev, Evgeny; Clemens, Jeremy; Jung, Michael; Clubb, Robert. "The structure of the Staphylococcus aureus sortase-substrate complex reveals how the universally conserved LPXTG sorting signal is recognized"  J. Biol. Chem. 284, 24465-24477 (2009).

Assembly members:
Sortase_A, polymer, 148 residues, 16753.145 Da.
Cbz-LPAT, polymer, 5 residues, 1298.356 Da.
CA, non-polymer, 40.078 Da.

Natural source:   Common Name: Firmicutes   Taxonomy ID: 1280   Superkingdom: Bacteria   Kingdom: not available   Genus/species: STAPHYLOCOCCUS AUREUS

Experimental source:   Production method: recombinant technology   Host organism: ESCHERICHIA COLI

Entity Sequences (FASTA):
Sortase_A: MQAKPQIPKDKSKVAGYIEI PDADIKEPVYPGPATPEQLN RGVSFAEENESLDDQNISIA GHTFIDRPNYQFTNLKAAKK GSMVYFKVGNETRKYKMTSI RDVKPTDVGVLDEQKGKDKQ LTLITCDDYNEKTGVWEKRK IFVATEVK
Cbz-LPAT: XLPAX

Data sets:
Data typeCount
13C chemical shifts636
15N chemical shifts157
1H chemical shifts1017

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1Sortase A1
2Cbz-LPAT*2
3Calcium3

Entities:

Entity 1, Sortase A 148 residues - 16753.145 Da.

1   METGLNALALYSPROGLNILEPROLYSASP
2   LYSSERLYSVALALAGLYTYRILEGLUILE
3   PROASPALAASPILELYSGLUPROVALTYR
4   PROGLYPROALATHRPROGLUGLNLEUASN
5   ARGGLYVALSERPHEALAGLUGLUASNGLU
6   SERLEUASPASPGLNASNILESERILEALA
7   GLYHISTHRPHEILEASPARGPROASNTYR
8   GLNPHETHRASNLEULYSALAALALYSLYS
9   GLYSERMETVALTYRPHELYSVALGLYASN
10   GLUTHRARGLYSTYRLYSMETTHRSERILE
11   ARGASPVALLYSPROTHRASPVALGLYVAL
12   LEUASPGLUGLNLYSGLYLYSASPLYSGLN
13   LEUTHRLEUILETHRCYSASPASPTYRASN
14   GLULYSTHRGLYVALTRPGLULYSARGLYS
15   ILEPHEVALALATHRGLUVALLYS

Entity 2, Cbz-LPAT* 5 residues - 1298.356 Da.

1   PHQLEUPROALAB27

Entity 3, Calcium - Ca - 40.078 Da.

1   CA

Samples:

sample_1: Sortase A, [U-100% 13C; U-100% 15N], 1 mM; Cbz-LPAT* 1 mM; TRIS 50 mM; sodium chloride 100 mM; Calcium Chloride 20 mM; sodium azide 0.01%; H2O 93%; D2O, [U-100% 2H], 7%

sample_2: Sortase A, [U-100% 15N], 1 mM; Cbz-LPAT* 1 mM; TRIS 50 mM; sodium chloride 100 mM; Calcium Chloride 20 mM; sodium azide 0.01%; H2O 93%; D2O, [U-100% 2H], 7%

sample_3: Sortase A, [U-100% 13C; U-100% 15N], 1 mM; Cbz-LPAT* 1 mM; TRIS 50 mM; sodium chloride 100 mM; Calcium Chloride 20 mM; sodium azide 0.01%; H2O 93%; D2O, [U-100% 2H], 7%

sample_conditions_1: ionic strength: 0.15 M; pH: 6.0; pressure: 1 atm; temperature: 302 K

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
3D 1H-15N NOESYsample_1isotropicsample_conditions_1
3D 1H-15N TOCSYsample_1isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D CBCA(CO)NHsample_3isotropicsample_conditions_1
3D C(CO)NHsample_3isotropicsample_conditions_1
3D HNCOsample_3isotropicsample_conditions_1
3D HNCACBsample_3isotropicsample_conditions_1
3D HBHA(CO)NHsample_3isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_3isotropicsample_conditions_1
3D HNHBsample_3isotropicsample_conditions_1
3D HCCH-COSYsample_3isotropicsample_conditions_1

Software:

X-PLOR NIH, Brunger A. T. et.al. - refinement

PIPP, Garrett - peak picking

NMRPipe, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

NMRDraw, Delaglio, Grzesiek, Vuister, Zhu, Pfeifer and Bax - data analysis

ProcheckNMR, Laskowski and MacArthur - refinement

Molmol, Koradi, Billeter and Wuthrich - structure solution

SPARKY, Goddard - peak picking

ATHNOS-CANDID, Herrmann, Guntert and Wuthrich - peak picking

NMR spectrometers:

  • BRUKER AVANCE 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 19624 19826
PDB
DBJ BAB43619 BAB58690 BAB96313 BAF68698 BAF79395
EMBL CAG41587 CAG44229 CAI82090 CAQ50958 CBI50513
GB AAD48437 AAW37316 ABD22861 ABD31836 ABQ50328
REF WP_000759357 WP_000759358 WP_000759359 WP_000759360 WP_000759361

Download simulated HSQC data in one of the following formats:
CSV: Backbone or all simulated shifts
SPARKY: Backbone or all simulated shifts