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TitleEnzymatic Basis for N-Glycan Sialylation: STRUCTURE OF RAT alpha 2,6-SIALYLTRANSFERASE (ST6GAL1) REVEALS CONSERVED AND UNIQUE FEATURES FOR GLYCAN SIALYLATION.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 34680-34698, Year 2013
Publish dateSep 13, 2013 (structure data deposition date)
AuthorsMeng, L. / Forouhar, F. / Thieker, D. / Gao, Z. / Ramiah, A. / Moniz, H. / Xiang, Y. / Seetharaman, J. / Milaninia, S. / Su, M. ...Meng, L. / Forouhar, F. / Thieker, D. / Gao, Z. / Ramiah, A. / Moniz, H. / Xiang, Y. / Seetharaman, J. / Milaninia, S. / Su, M. / Bridger, R. / Veillon, L. / Azadi, P. / Kornhaber, G. / Wells, L. / Montelione, G.T. / Woods, R.J. / Tong, L. / Moremen, K.W.
External linksJ. Biol. Chem. / PubMed:24155237
MethodsX-ray diffraction
Resolution2.4 Å
Structure data

PDB-4mps:
Crystal structure of rat Beta-galactoside alpha-2,6-sialyltransferase 1 (ST6GAL1), Northeast Structural Genomics Consortium Target RnR367A
Method: X-RAY DIFFRACTION / Resolution: 2.4 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-HOH:
WATER

Source
  • rattus norvegicus (Norway rat)
KeywordsTRANSFERASE / Structural Genomics / PSI-Biology / Northeast Structural Genomics Consortium / NESG / alpha-beta protein / Beta-galactoside alpha-2 / 6-sialyltransferase 1

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