Literature DB >> 15039582

Crystallization and preliminary X-ray analysis of the acyl carrier protein synthase (AcpS) from Staphylococcus aureus.

Dayna L Daubaras1, Eileen M Wilson, Todd Black, Corey Strickland, Brian M Beyer, Peter Orth.   

Abstract

Acyl carrier protein synthase (AcpS) catalyzes the transfer of 4'-phophopantetheine from coenzyme A to the acyl carrier protein (ACP) to activate it for fatty-acid biosynthesis. Two crystal forms of Staphylococcus aureus AcpS have been generated at 277 K using either NaCl or PEG 6000 as a precipitant. The diffraction patterns of the crystals extend to 1.65 and 1.8 A, respectively. Full sets of X-ray diffraction data were collected from native crystals and the crystal structures were solved by molecular replacement.

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Year:  2004        PMID: 15039582     DOI: 10.1107/S0907444904003282

Source DB:  PubMed          Journal:  Acta Crystallogr D Biol Crystallogr        ISSN: 0907-4449


  1 in total

1.  Acyl carrier protein synthases from gram-negative, gram-positive, and atypical bacterial species: Biochemical and structural properties and physiological implications.

Authors:  Kelly A McAllister; Robert B Peery; Genshi Zhao
Journal:  J Bacteriol       Date:  2006-07       Impact factor: 3.490

  1 in total

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