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© Institut Pasteur
Cells infected for 24 hrs with C. Trachomatis. The cell nuclei are labelled in blue, the bacteria appear yellow, within the inclusion lumen. A bacterial protein secreted out the inclusion into the host cytoplasm id labelled in red.
Publication : Acta crystallographica. Section F, Structural biology and crystallization communications

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

Team: Structural Microbiology
Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Acta crystallographica. Section F, Structural biology and crystallization communications - 22 Apr 2005

Guerin ME, Buschiazzo A, Korduláková J, Jackson M, Alzari PM

Link to Pubmed [PMID] – 16511084

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

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.