2WNB

Crystal Structure of a Mammalian Sialyltransferase in complex with disaccharide and CMP

Summary for 2WNB

• Entry DOI: 10.2210/pdb2wnb/pdb
• Related: 2WML 2WNF
• Related PRD ID: PRD_900084
• Descriptor: CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,3-sialyltransferase 1, beta-D-galactopyranose-(1-3)-2-acetamido-2-deoxy-alpha-D-galactopyranose, CYTIDINE-5'-MONOPHOSPHATE, ... (5 entities in total)
• Functional Keywords: glycosyltransferase, alternative splicing, disulfide bond, golgi apparatus, sialyltransferase, glycoprotein, signal-anchor, transmembrane, membrane, secreted, transferase, sialic acid
• Biological source: Sus scrofa (pig)
• Cellular location: Golgi apparatus, Golgi stack membrane; Single-pass type II membrane protein: Q02745
• Total number of polymer chains: 1
• Total formula weight: 35594.61

Authors

Rao, F.V.,Rich, J.R.,Raikic, B.,Wakarchuk, W.W.,Withers, S.G.,Strynadka, N.C.J. (deposition date: 2009-07-08, release date: 2009-10-13, Last modification date: 2024-10-09)

Primary citation

Rao, F.V.,Rich, J.R.,Rakic, B.,Buddai, S.,Schwartz, M.F.,Johnson, K.,Bowe, C.,Wakarchuk, W.W.,Defrees, S.,Withers, S.G.,Strynadka, N.C.J.
Structural Insight Into Mammalian Sialyltransferases.
Nat.Struct.Mol.Biol., 16:1186-, 2009

PubMed Abstract: Mammalian cell surfaces are modified by complex arrays of glycoproteins, glycolipids and polysaccharides, many of which terminate in sialic acid and have central roles in essential processes including cell recognition, adhesion and immunogenicity. Sialylation of glycoconjugates is performed by a set of sequence-related enzymes known as sialyltransferases (STs). Here we present the crystal structure of a mammalian ST, porcine ST3Gal-I, providing a structural basis for understanding the mechanism and specificity of these enzymes and for the design of selective inhibitors.

PubMed: 19820709
DOI: 10.1038/NSMB.1685

Experimental method

X-RAY DIFFRACTION (1.55 Å)