Literature DB >> 19923749

Expression, purification and crystallization of an archaeal-type phosphoenolpyruvate carboxylase.

Lakshmi Dharmarajan1, Jessica L Kraszewski, Biswarup Mukhopadhyay, Pete W Dunten.   

Abstract

An archaeal-type phosphoenolpyruvate carboxylase (PepcA) from Clostridium perfringens has been expressed in Escherichia coli in a soluble form with an amino-terminal His tag. The recombinant protein is enzymatically active and two crystal forms have been obtained. Complete diffraction data extending to 3.13 angstrom resolution have been measured from a crystal soaked in KAu(CN)(2), using radiation at a wavelength just above the Au L(III) edge. The asymmetric unit contains two tetramers of PepcA.

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Year:  2009        PMID: 19923749      PMCID: PMC2777057          DOI: 10.1107/S1744309109042663

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN: 1744-3091


  17 in total

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9.  The phosphoenolpyruvate carboxylase from Methanothermobacter thermautotrophicus has a novel structure.

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  1 in total

1.  Structure of an archaeal-type phosphoenolpyruvate carboxylase sensitive to inhibition by aspartate.

Authors:  Lakshmi Dharmarajan; Jessica L Kraszewski; Biswarup Mukhopadhyay; Pete W Dunten
Journal:  Proteins       Date:  2011-04-12
  1 in total

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