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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 May 1;61(Pt 5):518-20. Epub 2005 Apr 22.

Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis.

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1
Unité de Biochimie Structurale, CNRS URA 2185, Institut Pasteur, 75724 Paris Cedex 15, France.

Abstract

Phosphatidylinositol mannosyltransferase (PimA) is an essential enzyme for mycobacterial growth that catalyses the first mannosylation step in phosphatidyl-myo-inositol mannoside (PIM) biosynthesis. The enzyme belongs to the large GT4 family of glycosyltransferases, for which no structure is currently available. Recombinant purified PimA from Mycobacterium smegmatis has been crystallized in the presence of GDP and myo-inositol. The crystals belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 37.2, b = 72.4, c = 138.2 A, and diffract to 2.4 A resolution.

PMID:
16511084
PMCID:
PMC1952298
DOI:
10.1107/S1744309105012364
[Indexed for MEDLINE]
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