BMRB Entry 16270

Name: SOLUTION STRUCTURE OF THE S. AUREUS SORTASE A-SUBSTRATE COMPLEX
Published: 2009-07-16

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PDB ID: 2kid
Entry in NMR Restraints Grid
Validation report in NRG-CING
Chem Shift validation: AVS_anomalous, AVS_full, SPARTA
BMRB Entry DOI: doi:10.13018/BMR16270
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Bioinformatics (2015) 31 (8): 1322-1324 doi:10.1093/bioinformatics/btu829

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Title:

SOLUTION STRUCTURE OF THE S. AUREUS SORTASE A-SUBSTRATE COMPLEX

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:

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).
PubMed: 19592495

Assembly members:

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:

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

Experimental source:

Experimental source: Production method: recombinant technology Host organism: ESCHERICHIA COLI Vector: PET9A

Entity Sequences (FASTA):

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

Data sets:

assigned_chemical_shifts
- assigned_chem_shift_list_1

Data type	Count
13C chemical shifts	636
15N chemical shifts	157
1H chemical shifts	1017

Additional metadata:

Assembly
Samples and Experiments
Software
Spectrometers
Hide all

Assembly:

Entity Assembly ID	Entity Name	Entity ID
1	Sortase A	1
2	Cbz-LPAT*	2
3	Calcium	3

Entities:

Entity 1, Sortase A 148 residues - 16753.145 Da.

1

MET

GLN

ALA

LYS

PRO

GLN

ILE

PRO

LYS

ASP

2

LYS

SER

LYS

VAL

ALA

GLY

TYR

ILE

GLU

ILE

3

PRO

ASP

ALA

ASP

ILE

LYS

GLU

PRO

VAL

TYR

4

PRO

GLY

PRO

ALA

THR

PRO

GLU

GLN

LEU

ASN

5

ARG

GLY

VAL

SER

PHE

ALA

GLU

ASN

GLU

6

SER

LEU

ASP

GLN

ASN

ILE

SER

ILE

ALA

7

GLY

HIS

THR

PHE

ILE

ASP

ARG

PRO

ASN

TYR

8

GLN

PHE

THR

ASN

LEU

LYS

ALA

LYS

9

GLY

SER

MET

VAL

TYR

PHE

LYS

VAL

GLY

ASN

10

GLU

THR

ARG

LYS

TYR

LYS

MET

THR

SER

ILE

11

ARG

ASP

VAL

LYS

PRO

THR

ASP

VAL

GLY

VAL

12

LEU

ASP

GLU

GLN

LYS

GLY

LYS

ASP

LYS

GLN

13

LEU

THR

LEU

ILE

THR

CYS

ASP

TYR

ASN

14

GLU

LYS

THR

GLY

VAL

TRP

GLU

LYS

ARG

LYS

15

ILE

PHE

VAL

ALA

THR

GLU

VAL

LYS

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

1

PHQ

LEU

PRO

ALA

B27

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:

Name	Sample	Sample state	Sample conditions
2D 1H-15N HSQC	sample_2	isotropic	sample_conditions_1
2D 1H-13C HSQC	sample_3	isotropic	sample_conditions_1
3D 1H-15N NOESY	sample_1	isotropic	sample_conditions_1
3D 1H-15N TOCSY	sample_1	isotropic	sample_conditions_1
3D 1H-13C NOESY	sample_3	isotropic	sample_conditions_1
3D CBCA(CO)NH	sample_3	isotropic	sample_conditions_1
3D C(CO)NH	sample_3	isotropic	sample_conditions_1
3D HNCO	sample_3	isotropic	sample_conditions_1
3D HNCACB	sample_3	isotropic	sample_conditions_1
3D HBHA(CO)NH	sample_3	isotropic	sample_conditions_1
3D HCCH-TOCSY	sample_3	isotropic	sample_conditions_1
3D HNHA	sample_3	isotropic	sample_conditions_1
3D HNHB	sample_3	isotropic	sample_conditions_1
3D HCCH-COSY	sample_3	isotropic	sample_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

BMRB	19624 19826
PDB	1IJA 1T2O 1T2P 1T2W 2KID 2MLM
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