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› 6fgx

X-ray diffraction
2.9Å resolution

Crystal structure of the small alarmone synthethase 2 from Staphylococcus aureus bound to AMPCPP

Released:
DOI: 10.2210/pdb6fgx/pdb
Model geometry
Fit model/data
PDB entry 6fgx coloured by chain, front view.
PDB entry 6fgx coloured by chain, side view.
PDB entry 6fgx coloured by chain, top view.
Source organism: Staphylococcus aureus
Primary publication:
Structural and mechanistic divergence of the small (p)ppGpp synthetases RelP and RelQ.
Steinchen W, Vogt MS, Altegoer F, Giammarinaro PI, Horvatek P, Wolz C, Bange G
OpenAccess logo Sci Rep 8 2195 (2018)
PMID: 29391580

Function and Biology Details

Reaction catalysed: 
GTP + ATP = guanosine 3'-diphosphate 5'-triphosphate + AMP.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo tetramer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-197814 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RelA/SpoT domain-containing protein Chains: A, B
Molecule details ›
Chains: A, B
Length: 237 amino acids
Theoretical weight: 28.09 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: W8U368 (Residues: 2-230; Coverage: 100%)
Gene names: ACR79_11720, AS572_08785, CNH36_14055, CV021_15105, DQU50_12290, E1948_07175, E1948_13295, EIG94_08155, EIH03_07215, EP54_00695, EQ90_03295, ERS391062_01539, G0Z31_03585, G6Y24_11435, GAY54_09280, GF599_04865, GO814_08755, GO942_11055, GQX37_12820, GQX52_00055, GZ130_11835, GZ164_11915, H2649_03735, HH313_002590, LB359_10550, M1K003_1970, NCTC13131_00008, NCTC6133_03360, NCTC7972_02139, NCTC8317_02445, SAMEA1029512_00011, SAMEA1029528_00871, SAMEA1466929_02234, SAMEA2078260_01114, SAMEA2078588_01184, SAMEA2080344_00628, SAMEA2081063_00952, SAMEA4008575_00779, SAMEA4552975_01927, SAMEA70146418_00228, SAMEA70153168_01185, SAMEA70245418_00278, ywaC, ywaC_1
Sequence domains: Region found in RelA / SpoT proteins
Structure domains: Beta Polymerase, domain 2

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand APC 2 x APC
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ESRF BEAMLINE ID29
Spacegroup: I4122
Unit cell:
a: 125.862Å b: 125.862Å c: 217.879Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.223 0.223 0.262
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

Make and break the alarmone: regulation of (p)ppGpp synthetase/hydrolase enzymes in bacteria.
Ronneau et al. (2019)
4 more

2 mentions without citation

Structural and mechanistic divergence of the small (p)ppGpp synthetases RelP and RelQ.
Steinchen et al. (2018)
1 more