The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14
- Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10065 (United States)
- Howard Hughes Medical Institute, Laboratory of Genetically Encoded Small Molecules, The Rockefeller University, 1230 York Avenue, New York, NY 10065 (United States)
The 2.7 Å resolution crystal structure of Teg14, a glycopeptide sulfotransferase cloned from an uncultured soil bacterium, is described. The relationship of Teg14 to other sulfotransferases is discussed. The TEG gene cluster was recently isolated from an environmental DNA library and is predicted to encode the biosynthesis of a polysulfated glycopeptide congener. Three closely related sulfotransferases found in the TEG gene cluster (Teg12, Teg13 and Teg14) have been shown to sulfate the teicoplanin aglycone at three unique sites. Crystal structures of the first sulfotransferase from the TEG cluster, Teg12, in complex with the teicoplanin aglycone and its desulfated cosubstrate PAP have recently been reported [Bick et al. (2010 ▶), Biochemistry, 49, 4159–4168]. Here, the 2.7 Å resolution crystal structure of the apo form of Teg14 is reported. Teg14 sulfates the hydroxyphenylglycine at position 4 in the teicoplanin aglycone. The Teg14 structure is discussed and is compared with those of other bacterial 3′-phosphoadenosine 5′-phosphosulfate-dependent sulfotransferases facilitating crystallographic experiments, especially in the field of microcrystallography.
- OSTI ID:
- 22351224
- Journal Information:
- Acta Crystallographica. Section D: Biological Crystallography, Vol. 66, Issue Pt 12; Other Information: PMCID: PMC2995723; PMID: 21123867; PUBLISHER-ID: ea5130; OAI: oai:pubmedcentral.nih.gov:2995723; Copyright (c) International Union of Crystallography 2010; Country of input: International Atomic Energy Agency (IAEA); ISSN 0907-4449
- Country of Publication:
- Denmark
- Language:
- English
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