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

Goyal, Aneesh ; Yousuf, Malikmohamed ; Arora, Pooja ; Gokhale, Rajesh S. ; Rajakumara, Eerappa ; Sankaranarayanan, Rajan (2006) Crystallization and preliminary X-ray crystallographic studies of the N-terminal domain of FadD28, a fatty-acyl AMP ligase from Mycobacterium tuberculosis Acta Crystallographica Section F, 62 (4). pp. 350-352. ISSN 1744-3091

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Official URL: http://onlinelibrary.wiley.com/doi/10.1107/S174430...

Related URL: http://dx.doi.org/10.1107/S1744309106005938

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 P212121, with unit-cell parameters a = 50.97, b = 60.74, c = 136.54 Å. The crystal structure of the N-terminal domain of FadD28 at 2.35 Å resolution has been solved using the MAD method.

Item Type:Article
Source:Copyright of this article belongs to International Union of Crystallography.
Keywords:FadD28; Fatty-acyl AMP Ligase (FALL); Phthiocerol Dimycocerosate (PDIM); Mycobacterium tuberculosis
ID Code:23104
Deposited On:25 Nov 2010 13:32
Last Modified:02 Jun 2011 07:00

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