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Biochem Biophys Res Commun. 2003 Jun 13;305(4):997-1001.

Crystallization and characterization of polyphosphate kinase from Escherichia coli.

Author information

1
Department of Biological Structure, University of Washington, Seattle, WA 98195, USA.

Abstract

Linear polyphosphate chains have been found to play a key role in bacterial responses to stresses and nutritional depletion, and are necessary for host infection of various pathogens. Polyphosphate kinase (PPK) is a critical enzyme responsible for polyphosphate synthesis in bacteria. PPK knockout mutations in several Gram-negative pathogens identify PPK as an ideal drug target for the development of a new class of antibacterial drugs. To reveal the catalytic mechanism and provide a structural basis for drug discovery, we have purified and crystallized full-length Escherichia coli PPK and its complex with AMP-PNP. The crystals diffract to a resolution of 2.5A and belong to the space group P4(2)2(1)2 with unit-cell parameters a=152.0, b=152.0, and c=150.0 A. Crystal structure of PPK is being determined by the Se-Met MAD experiment.

PMID:
12767929
DOI:
10.1016/s0006-291x(03)00886-6
[Indexed for MEDLINE]

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