3EWI

Structural analysis of the C-terminal domain of murine CMP-Sialic acid Synthetase

Summary for 3EWI

• Entry DOI: 10.2210/pdb3ewi/pdb
• Related: 1QWJ
• Descriptor: N-acylneuraminate cytidylyltransferase (2 entities in total)
• Functional Keywords: beta barrel, had-like, rossmannoid fold, nucleotidyltransferase, nucleus, transferase
• Biological source: Mus Musculus (mouse)
• Cellular location: Nucleus : Q99KK2
• Total number of polymer chains: 2
• Total formula weight: 36744.59

Authors

Oschlies, M.,Dickmanns, A.,Stummeyer, K.,Gerardy-Schahn, R.,Ficner, R.,Muenster-Kuehnel, A.K. (deposition date: 2008-10-15, release date: 2009-08-18, Last modification date: 2023-12-27)

• Primary citation: Oschlies, 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.; A C-terminal phosphatase module conserved in vertebrate CMP-sialic acid synthetases provides a tetramerization interface for the physiologically active enzyme.; J.Mol.Biol., 393:83-97, 2009; PubMed: 19666032; DOI: 10.1016/j.jmb.2009.08.003

Experimental method

X-RAY DIFFRACTION (1.9 Å)