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 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.

Cite this paper

@article{Guerin2005CrystallizationAP, title={Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis.}, author={Marcelo E Guerin and Alejandro Buschiazzo and Jana Kordul{\'a}kov{\'a} and Mary Jackson and Pedro M Alzari}, journal={Acta crystallographica. Section F, Structural biology and crystallization communications}, year={2005}, volume={61 Pt 5}, pages={518-20} }