1TEX

Mycobacterium smegmatis Stf0 Sulfotransferase with Trehalose

Summary for 1TEX

• Entry DOI: 10.2210/pdb1tex/pdb
• Related PRD ID: PRD_900006
• Descriptor: Stf0 Sulfotransferase, alpha-D-glucopyranose-(1-1)-alpha-D-glucopyranose (3 entities in total)
• Functional Keywords: mycobacterium, sulfotransferase, sulfolipid, sulfation, trehalose, trehalose-2-sulfate, transferase
• Biological source: Mycobacterium smegmatis
• Total number of polymer chains: 4
• Total formula weight: 131359.22

Authors

Mougous, J.D.,Petzold, C.J.,Senaratne, R.H.,Lee, D.H.,Akey, D.L.,Lin, F.L.,Munchel, S.E.,Pratt, M.R.,Riley, L.W.,Leary, J.A.,Berger, J.M.,Bertozzi, C.R. (deposition date: 2004-05-25, release date: 2004-07-20, Last modification date: 2024-02-14)

Primary citation

Mougous, J.D.,Petzold, C.J.,Senaratne, R.H.,Lee, D.H.,Akey, D.L.,Lin, F.L.,Munchel, S.E.,Pratt, M.R.,Riley, L.W.,Leary, J.A.,Berger, J.M.,Bertozzi, C.R.
Identification, function and structure of the mycobacterial sulfotransferase that initiates sulfolipid-1 biosynthesis.
Nat.Struct.Mol.Biol., 11:721-729, 2004

PubMed Abstract: 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.

PubMed: 15258569
DOI: 10.1038/nsmb802

Experimental method

X-RAY DIFFRACTION (2.6 Å)