Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis
Journal Article
·
· Acta Crystallographica. Section F
- Unité de Biochimie Structurale (CNRS URA 2185), Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris CEDEX 15 (France)
- Unité de Génétique Mycobacterienne, Institut Pasteur, 25 Rue du Dr Roux, 75724 Paris CEDEX 15 (France)
Mycobacterial PimA is an essential enzyme that catalyses the first mannosylation step in phosphatidyl-myo-inositol mannoside (PIM) biosynthesis. Crystals of the enzyme from M. smegmatis, obtained in the presence of GDP and myo-inositol, are orthorhombic (P2{sub 1}2{sub 1}2{sub 1}) and diffract X-rays to 2.4 Å resolution. 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{sub 1}2{sub 1}2{sub 1}, with unit-cell parameters a = 37.2, b = 72.4, c = 138.2 Å, and diffract to 2.4 Å resolution.
- OSTI ID:
- 22355994
- Journal Information:
- Acta Crystallographica. Section F, Journal Name: Acta Crystallographica. Section F Journal Issue: Pt 5 Vol. 61; ISSN ACSFCL; ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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