Crystallization and preliminary crystallographic analysis of PimA, an essential mannosyltransferase from Mycobacterium smegmatis.
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.
Guerin
Marcelo E
ME
Unité de Biochimie Structurale, CNRS URA 2185, Institut Pasteur, 75724 Paris Cedex 15, France.
Buschiazzo
Alejandro
A
Korduláková
Jana
J
Jackson
Mary
M
Alzari
Pedro M
PM
D003460:Crystallization; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D008364:Mannosyltransferases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D020102:Mycobacterium smegmatis / Q000201:enzymology* / Q000378:metabolism; D010716:Phosphatidylinositols / Q000096:biosynthesis / Q000737:chemistry; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
D010716:Phosphatidylinositols; D011994:Recombinant Proteins; C034154:phosphatidylinositol mannoside; D008364:Mannosyltransferases