Literature DB >> 16582482

Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis.

Aneesh Goyal1, Malikmohamed Yousuf, Eerappa Rajakumara, Pooja Arora, Rajesh S Gokhale, Rajan Sankaranarayanan.   

Abstract

FadD28 from Mycobacterium tuberculosis belongs to the fatty-acyl AMP ligase (FAAL) family of proteins. It is essential for the biosynthesis of a virulent phthiocerol dimycocerosate (PDIM) lipid that is only found in the cell wall of pathogenic mycobacteria. The N-terminal domain, comprising of the first 460 residues, was crystallized by the hanging-drop vapour-diffusion method at 295 K. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 angstroms. The crystal structure of the N-terminal domain of FadD28 at 2.35 angstroms resolution has been solved using the MAD method.

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Year:  2006        PMID: 16582482      PMCID: PMC2222565          DOI: 10.1107/S1744309106005938

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


  15 in total

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  8 in total

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8.  Mechanistic and functional insights into fatty acid activation in Mycobacterium tuberculosis.

Authors:  Pooja Arora; Aneesh Goyal; Vivek T Natarajan; Eerappa Rajakumara; Priyanka Verma; Radhika Gupta; Malikmohamed Yousuf; Omita A Trivedi; Debasisa Mohanty; Anil Tyagi; Rajan Sankaranarayanan; Rajesh S Gokhale
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  8 in total

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