BMRB Entry 16811

Title:
Solution Structure of Bacillus anthracis Sortase A (SrtA) Transpeptidase
Deposition date:
2010-03-31
Original release date:
2010-05-28
Authors:
Weiner, Ethan; Robson, Scott; Marohn, Melanie; Clubb, Robert
Citation:

Citation: Weiner, Ethan; Robson, Scott; Marohn, Melanie; Clubb, Robert. "The Sortase A enzyme that attaches proteins to the cell wall of Bacillus anthracis contains an unusual active site architecture."  J. Biol. Chem. 285, 23433-23443 (2010).
PubMed: 20489200

Assembly members:

Assembly members:
SrtA, polymer, 158 residues, 17110.521 Da.

Natural source:

Natural source:   Common Name: Bacillus anthracis   Taxonomy ID: 1392   Superkingdom: Bacteria   Kingdom: not available   Genus/species: Bacillus anthracis

Experimental source:

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

Data sets:
Data typeCount
13C chemical shifts592
15N chemical shifts146
1H chemical shifts962

Additional metadata:

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

Assembly:

Entity Assembly IDEntity NameEntity ID
1SrtA1

Entities:

Entity 1, SrtA 158 residues - 17110.521 Da.

Residues 52-56 represent a non-native affinity tag

1   GLYSERHISMETASPALASERLYSILEASP
2   GLNPROASPLEUALAGLUVALALAASNALA
3   SERLEUASPLYSLYSGLNVALILEGLYARG
4   ILESERILEPROSERVALSERLEUGLULEU
5   PROVALLEULYSSERSERTHRGLULYSASN
6   LEULEUSERGLYALAALATHRVALLYSGLU
7   ASNGLNVALMETGLYLYSGLYASNTYRALA
8   LEUALAGLYHISASNMETSERLYSLYSGLY
9   VALLEUPHESERASPILEALASERLEULYS
10   LYSGLYASPLYSILETYRLEUTYRASPASN
11   GLUASNGLUTYRGLUTYRALAVALTHRGLY
12   VALSERGLUVALTHRPROASPLYSTRPGLU
13   VALVALGLUASPHISGLYLYSASPGLUILE
14   THRLEUILETHRCYSVALSERVALLYSASP
15   ASNSERLYSARGTYRVALVALALAGLYASP
16   LEUVALGLYTHRLYSALALYSLYS

Samples:

sample_1: SrtA, [U-100% 15N], 4 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_2: SrtA, [U-100% 13C; U-100% 15N], 2.5 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

sample_3: SrtA, [U-100% 13C; U-100% 15N], 2.5 mM; MES 10 mM; Bis-Tris 20 mM; H2O 93%; D2O 7%

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

Experiments:

NameSampleSample stateSample conditions
2D 1H-15N HSQCsample_1isotropicsample_conditions_1
2D 1H-13C HSQCsample_3isotropicsample_conditions_1
2D 1H-13C HSQCsample_2isotropicsample_conditions_1
3D CBCA(CO)NHsample_2isotropicsample_conditions_1
3D C(CO)NHsample_2isotropicsample_conditions_1
3D HNCOsample_2isotropicsample_conditions_1
3D HNCAsample_2isotropicsample_conditions_1
3D HNCACBsample_2isotropicsample_conditions_1
3D HBHA(CO)NHsample_2isotropicsample_conditions_1
3D HCCH-TOCSYsample_3isotropicsample_conditions_1
3D HNHAsample_2isotropicsample_conditions_1
3D 1H-15N NOESYsample_2isotropicsample_conditions_1
3D 1H-13C NOESYsample_3isotropicsample_conditions_1
3D HNHBsample_2isotropicsample_conditions_1
3D HCCH-COSYsample_2isotropicsample_conditions_1
3D HCACOsample_2isotropicsample_conditions_1
4D 15N-13C HMQC-NOESY-HSQCsample_2isotropicsample_conditions_1
2D (HB)CB(CGCDCE)HEsample_2isotropicsample_conditions_1
2D (HB)CB(CGCD)HDsample_2isotropicsample_conditions_1
2D 1H-15N HSQCsample_2isotropicsample_conditions_1
2D 1H-15N HSQC NOE with interleaved presat and no satsample_1isotropicsample_conditions_1

Software:

X-PLOR NIH, Schwieters, Kuszewski, Tjandra and Clore - refinement

PIPP, Garrett - peak picking

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

ATHNOS-CANDID, Herrmann, Guntert, Wuthrich - chemical shift assignment

ModelFree, Palmer - data analysis

ProcheckNMR, Laskowski and MacArthur - geometry optimization

TALOS, Cornilescu, Delaglio and Bax - geometry optimization

xwinnmr, Bruker Biospin - collection

CARA, Keller - chemical shift assignment

NMR spectrometers:

  • Bruker Avance 500 MHz
  • Bruker Avance 600 MHz
  • Bruker Avance 800 MHz

Related Database Links:

BMRB 11570 26510
PDB
DBJ BAL16456 BAR78533 GAE96182 GAO57723 GAO63420
EMBL CJA38300 CJJ39486 CKE38654 CKE81514 CKE96545
GB AAP24701 AAS39688 AAT29792 AAT52982 AAU19641
REF NP_843215 WP_001041406 WP_001041710 WP_001041711 WP_001041715

Download HSQC peak lists in one of the following formats:
CSV: Backbone or all simulated peaks
SPARKY: Backbone or all simulated peaks