› 9clo

Electron Microscopy
3.1Å resolution

DosP R97A with c-di-GMP

Released:
DOI: 10.2210/pdb9clo/pdb
PDB entry 9clo coloured by chain, front view.
PDB entry 9clo coloured by chain, side view.
PDB entry 9clo coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structures of the multi-domain oxygen sensor DosP: remote control of a c-di-GMP phosphodiesterase by a regulatory PAS domain.
Wu W, Kumar P, Brautigam CA, Tso SC, Baniasadi HR, Kober DL, Gilles-Gonzalez MA
Nat Commun 15 9653 (2024)
PMID: 39511182
Related structures: EMD-45727

Function and Biology Details

Reaction catalysed: 
Cyclic di-3',5'-guanylate + H(2)O = 5'-phosphoguanylyl(3'->5')guanosine
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160054 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Oxygen sensor protein DosP Chains: A, B
Molecule details ›
Chains: A, B
Length: 787 amino acids
Theoretical weight: 89 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P76129 (Residues: 12-798; Coverage: 99%)
Gene names: JW1484, b1489, dos, dosP, pdeO, yddU
Sequence domains:

Ligands and Environments


Cofactor: Ligand HEM 2 x HEM
2 bound ligands:
Ligand C2E 2 x C2E
Ligand MG 4 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.1Å
Relevant EMDB volumes: EMD-45727
Expression system: Escherichia coli

Quick links

Experimental raw data

Links to raw experimental data available for this entry are listed below

Electron microscopy data related to PDB entry 9clo found at the Electron Microscopy Public Image Archive (EMPIAR)

Data DOI: 10.6019/EMPIAR-12205
Datasets: 1
Total size: 4300Gb
EMPIAR thumbnail