› 6rpu

X-ray diffraction
2.11Å resolution

Structure of the ternary complex of the IMPDH enzyme from Ashbya gossypii bound to the dinucleoside polyphosphate Ap5G and GDP

Released:
DOI: 10.2210/pdb6rpu/pdb
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PDB entry 6rpu coloured by chain, front view.
PDB entry 6rpu coloured by chain, side view.
PDB entry 6rpu coloured by chain, top view.
Source organism: Eremothecium gossypii ATCC 10895
Primary publication:
The Bateman domain of IMP dehydrogenase is a binding target for dinucleoside polyphosphates.
Fernández-Justel D, Peláez R, Revuelta JL, Buey RM
J Biol Chem 294 14768-14775 (2019)
PMID: 31416831

Function and Biology Details

Reaction catalysed: 
Inosine 5'-phosphate + NAD(+) + H(2)O = xanthosine 5'-phosphate + NADH
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181105 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Inosine-5'-monophosphate dehydrogenase Chain: A
Molecule details ›
Chain: A
Length: 522 amino acids
Theoretical weight: 56.53 KDa
Source organism: Eremothecium gossypii ATCC 10895
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q756Z6 (Residues: 1-522; Coverage: 100%)
Gene name: AGOS_AER117W
Sequence domains:

Ligands and Environments

3 bound ligands:
Ligand G5P 1 x G5P
Ligand GDP 1 x GDP
Ligand ACT 4 x ACT
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: ALBA BEAMLINE XALOC
Spacegroup: I422
Unit cell:
a: 148.538Å b: 148.538Å c: 103.828Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.255 0.254 0.284
Expression system: Escherichia coli BL21

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Citations

4 review citations

Re-evaluation of Diadenosine Tetraphosphate (Ap4A) From a Stress Metabolite to Bona Fide Secondary Messenger.
Ferguson et al. (2020)
3 more

4 mentions without citation

The gateway to guanine nucleotides: Allosteric regulation of IMP dehydrogenases.
Buey et al. (2022)
3 more

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