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

Authors :
Goyal, Aneesh
Yousuf, Malikmohamed
Rajakumara, Eerappa
Arora, Pooja
Gokhale, Rajesh S.
Sankaranarayanan, Rajan
Source :
Acta Crystallographica: Section F (Wiley-Blackwell); Apr2006, Vol. 62 Issue 4, p350-352, 3p, 1 Color Photograph, 1 Black and White Photograph, 1 Chart
Publication Year :
2006

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<subscript>1</subscript>2<subscript>1</subscript>2<subscript>1</subscript>, 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. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
17443091
Volume :
62
Issue :
4
Database :
Complementary Index
Journal :
Acta Crystallographica: Section F (Wiley-Blackwell)
Publication Type :
Academic Journal
Accession number :
20386449
Full Text :
https://doi.org/10.1107/S1744309106005938