1XDP

Crystal Structure of the E.coli Polyphosphate Kinase in complex with AMPPNP

Summary for 1XDP

• Entry DOI: 10.2210/pdb1xdp/pdb
• Related: 1XDO
• Descriptor: Polyphosphate kinase, MAGNESIUM ION, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: e.coli polyphosphate kinase, ppk, ppk complex with amppnp, amppnp, transferase
• Biological source: Escherichia coli
• Cellular location: Cell inner membrane ; Peripheral membrane protein : P0A7B1
• Total number of polymer chains: 2
• Total formula weight: 161940.05

Authors

Zhu, Y.,Huang, W.,Lee, S.S.,Xu, W. (deposition date: 2004-09-07, release date: 2005-06-21, Last modification date: 2024-02-14)

Primary citation

Zhu, Y.,Huang, W.,Lee, S.S.,Xu, W.
Crystal structure of a polyphosphate kinase and its implications for polyphosphate synthesis
Embo Rep., 6:681-687, 2005

PubMed Abstract: 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.

PubMed: 15947782
DOI: 10.1038/sj.embor.7400448

Experimental method

X-RAY DIFFRACTION (2.5 Å)