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TitleA C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme.
Journal, issue, pagesJ. Mol. Biol., Vol. 393, Page 83-97, Year 2009
Publish dateOct 15, 2008 (structure data deposition date)
AuthorsOschlies, M. / Dickmanns, A. / Haselhorst, T. / Schaper, W. / Stummeyer, K. / Tiralongo, J. / Weinhold, B. / Gerardy-Schahn, R. / von Itzstein, M. / Ficner, R. / Munster-Kuhnel, A.K.
External linksJ. Mol. Biol. / PubMed:19666032
MethodsX-ray diffraction
Resolution1.9 Å
Structure data

PDB-3ewi:
Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase
Method: X-RAY DIFFRACTION / Resolution: 1.9 Å

Chemicals

ChemComp-HOH:
WATER

Source
  • mus musculus (house mouse)
KeywordsTRANSFERASE / beta barrel / HAD-like / rossmannoid fold / Nucleotidyltransferase / Nucleus

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