PMID:12767929

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Citation

Zhu, Y, Lee, SS and Xu, W (2003) Crystallization and characterization of polyphosphate kinase from Escherichia coli. Biochem. Biophys. Res. Commun. 305:997-1001

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.

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Keywords

Adenylyl Imidodiphosphate/metabolism; Crystallography, X-Ray; Escherichia coli/enzymology; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/metabolism; Escherichia coli Proteins/ultrastructure; Phosphotransferases (Alcohol Group Acceptor)/chemistry; Phosphotransferases (Alcohol Group Acceptor)/metabolism; Phosphotransferases (Alcohol Group Acceptor)/ultrastructure; Phosphotransferases (Phosphate Group Acceptor)/chemistry; Phosphotransferases (Phosphate Group Acceptor)/metabolism; Phosphotransferases (Phosphate Group Acceptor)/ultrastructure; Solubility

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