› 6gyz

X-ray diffraction
3Å resolution

Crystal structure of GlmM from Staphylococcus aureus

Released:
DOI: 10.2210/pdb6gyz/pdb
PDB 6gyz coloured by chain and viewed from the front.
PDB 6gyz coloured by chain and viewed from the side.
PDB 6gyz coloured by chain and viewed from the top.
Source organism: Staphylococcus aureus
Primary publication:
Inhibition of the Staphylococcus aureus c-di-AMP cyclase DacA by direct interaction with the phosphoglucosamine mutase GlmM.
Tosi T, Hoshiga F, Millership C, Singh R, Eldrid C, Patin D, Mengin-Lecreulx D, Thalassinos K, Freemont P, Gründling A
PLoS Pathog. 15 e1007537 (2019)
PMID: 30668586

Function and Biology Details

Reaction catalysed: 
Alpha-D-glucosamine 1-phosphate = D-glucosamine 6-phosphate
Biochemical function:
Biological process:
  • not assigned
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Phosphoglucosamine mutase Chains: A, B
Molecule details ›
Chains: A, B
Length: 455 amino acids
Theoretical weight: 49.78 KDa
Source organism: Staphylococcus aureus
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A0D6H967 (Residues: 1-451; Coverage: 100%)
Gene names: DD547_02193, EDCC5055_02130, EP54_06960, EQ90_12990, FA040_09780, GO814_05610, GQX37_13415, HMPREF3211_00023, NCTC10702_03404, NCTC13131_01495, SAGV69_02603, SAHC1335_00106, SAMEA2077334_01939, SAMEA2078260_01954, SAMEA2078588_01925, SAMEA2080344_01761, SAMEA2081063_01776, SAMEA2081470_01686, SAMEA70146418_02176, glmM, glmM_1
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: DIAMOND BEAMLINE I03
Spacegroup: P212121
Unit cell:
a: 88.653Å b: 93.884Å c: 156.308Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.224 0.222 0.273
Expression system: Escherichia coli

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Citations

1 review citation

Cyclic di-AMP, a second messenger of primary importance: tertiary structures and binding mechanisms.
He et al. (2020)
11 other articles