Structural Biology and Crystallization Communications Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis - Institut Pasteur Access content directly
Journal Articles Acta Crystallographica Section F: Structural Biology and Crystallization Communications Year : 2005

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

Abstract

Phosphatidylinositol mannosyltransferase (PimA) is an essential enzyme for mycobacterial growth that catalyses the first mannosylation step in phospha-tidyl-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 Å , and diffract to 2.4 Å resolution.

Dates and versions

pasteur-02554105 , version 1 (25-04-2020)

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Marcelo E Guerin, Alejandro Buschiazzo, Jana Korduláková, Mary Jackson, Pedro Alzari. Structural Biology and Crystallization Communications Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis. Acta Crystallographica Section F: Structural Biology and Crystallization Communications, 2005, 61 (5), pp.518-520. ⟨10.1107/S1744309105012364⟩. ⟨pasteur-02554105⟩

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