1tex
From Proteopedia
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Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose
Overview
Sulfolipid-1 (SL-1) is an abundant sulfated glycolipid and potential, virulence factor found in Mycobacterium tuberculosis. SL-1 consists of a, trehalose-2-sulfate (T2S) disaccharide elaborated with four lipids. We, identified and characterized a conserved mycobacterial sulfotransferase, Stf0, which generates the T2S moiety of SL-1. Biochemical studies, demonstrated that the enzyme requires unmodified trehalose as substrate, and is sensitive to small structural perturbations of the disaccharide., Disruption of stf0 in Mycobacterium smegmatis and M. tuberculosis resulted, in the loss of T2S and SL-1 formation, respectively. The structure of Stf0, at a resolution of 2.6 A reveals the molecular basis of trehalose, recognition and a unique dimer configuration that encloses the substrate, into a bipartite active site. These data provide strong evidence that Stf0, carries out the first committed step in the biosynthesis of SL-1 and, establish a system for probing the role of SL-1 in M. tuberculosis, infection.
About this Structure
1TEX is a Single protein structure of sequence from Mycobacterium smegmatis with TRE as ligand. Full crystallographic information is available from OCA.
Reference
Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis., Mougous JD, Petzold CJ, Senaratne RH, Lee DH, Akey DL, Lin FL, Munchel SE, Pratt MR, Riley LW, Leary JA, Berger JM, Bertozzi CR, Nat Struct Mol Biol. 2004 Aug;11(8):721-9. Epub 2004 Jul 18. PMID:15258569
Page seeded by OCA on Sun Nov 25 02:06:34 2007
Categories: Mycobacterium smegmatis | Single protein | Akey, D.L. | Berger, J.M. | Bertozzi, C.R. | Leary, J.A. | Lee, D.H. | Lin, F.L. | Mougous, J.D. | Munchel, S.E. | Petzold, C.J. | Pratt, M.R. | Riley, L.W. | Senaratne, R.H. | TRE | Mycobacterium | Sulfation | Sulfolipid | Sulfotransferase | Trehalose | Trehalose-2-sulfate
