1XDO: Crystal Structure Of Escherichia Coli Polyphosphate Kinase

Polyphosphate (polyP), a linear polymer of hundreds of orthophosphate residues, exists in all tested cells in nature, from pathogenic bacteria to mammals. In bacteria, polyP has a crucial role in stress responses and stationary-phase survival. Polyphosphate kinase (PPK) is the principal enzyme that catalyses the synthesis of polyP in bacteria. It has been shown that PPK is required for bacterial motility, biofilm formation and the production of virulence factors. PPK inhibitors may thus provide a unique therapeutic opportunity against antibiotic-resistant pathogens. Here, we report crystal structures of full-length Escherichia coli PPK and its complex with AMPPNP (beta-gamma-imidoadenosine 5-phosphate). PPK forms an interlocked dimer, with each 80 kDa monomer containing four structural domains. The PPK active site is located in a tunnel, which contains a unique ATP-binding pocket and may accommodate the translocation of synthesized polyP. The PPK structure has laid the foundation for understanding the initiation of polyP synthesis by PPK.
PDB ID: 1XDODownload
MMDB ID: 34955
PDB Deposition Date: 2004/9/7
Updated in MMDB: 2014/11
Experimental Method:
x-ray diffraction
Resolution: 3  Å
Source Organism:
Similar Structures:
Biological Unit for 1XDO: dimeric; determined by author and by software (PISA)
Molecular Components in 1XDO
Label Count Molecule
Proteins (2 molecules)
Polyphosphate Kinase(Gene symbol: ppk)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB