The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14

Bick, Matthew J.; Banik, Jacob J.; Darst, Seth A.

doi:10.1107/S0907444910036681

Title: The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14

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Abstract

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.

Authors:

Bick, Matthew J. ^[1]; Banik, Jacob J. ^[2]; Darst, Seth A. ^[1]

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)

Publication Date:: Wed Dec 01 00:00:00 EST 2010

OSTI Identifier:: 22351224

Resource Type:: Journal Article

Journal Name:: Acta Crystallographica. Section D: Biological Crystallography

Additional Journal Information:: Journal Volume: 66; Journal 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); Journal ID: ISSN 0907-4449

Country of Publication:: Denmark

Language:: English

Subject:: 75 CONDENSED MATTER PHYSICS, SUPERCONDUCTIVITY AND SUPERFLUIDITY; CRYSTAL STRUCTURE; DNA; IRON; RESOLUTION; SULFATES

Citation Formats


                    Bick, Matthew J., Banik, Jacob J., Darst, Seth A., Brady, Sean F., E-mail: sbrady@rockefeller.edu, and Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10065. The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14.  Denmark: N. p., 2010. 
        Web.  doi:10.1107/S0907444910036681.

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                    Bick, Matthew J., Banik, Jacob J., Darst, Seth A., Brady, Sean F., E-mail: sbrady@rockefeller.edu, & Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10065. The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14.  Denmark.  https://doi.org/10.1107/S0907444910036681

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                    Bick, Matthew J., Banik, Jacob J., Darst, Seth A., Brady, Sean F., E-mail: sbrady@rockefeller.edu, and Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10065. 2010.  
        "The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14".  Denmark.  https://doi.org/10.1107/S0907444910036681.

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@article{osti_22351224,

  title        = {The 2.7 Å resolution structure of the glycopeptide sulfotransferase Teg14},

  author       = {Bick, Matthew J. and Banik, Jacob J. and Darst, Seth A. and Brady, Sean F., E-mail: sbrady@rockefeller.edu and Laboratory of Molecular Biophysics, The Rockefeller University, 1230 York Avenue, New York, NY 10065},

  abstractNote = {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.},

  doi          = {10.1107/S0907444910036681},

  url          = {https://www.osti.gov/biblio/22351224},
  journal      = {Acta Crystallographica. Section D: Biological Crystallography},

  issn         = {0907-4449},

  number       = Pt 12,

  volume       = 66,

  place        = {Denmark},

  year         = {Wed Dec 01 00:00:00 EST 2010},

  month        = {Wed Dec 01 00:00:00 EST 2010}

}

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