2J0B

Structure of the catalytic domain of mouse Manic Fringe in complex with UDP and manganese

Summary for 2J0B

Entry DOI	10.2210/pdb2j0b/pdb
Related	2J0A
Descriptor	BETA-1,3-N-ACETYLGLUCOSAMINYLTRANSFERASE MANIC FRINGE, SULFATE ION, POTASSIUM ION, ... (6 entities in total)
Functional Keywords	glycosyltransferase, developmental protein, transmembrane, golgi apparatus, notch signaling, membrane, transferase, glycoprotein, signal-anchor
Biological source	MUS MUSCULUS (MOUSE)
Total number of polymer chains	1
Total formula weight	32143.55
Authors	Jinek, M.,Chen, Y.-W.,Clausen, H.,Cohen, S.M.,Conti, E. (deposition date: 2006-08-01, release date: 2006-09-04, Last modification date: 2024-10-23)
Primary citation	Jinek, M.,Chen, Y.-W.,Clausen, H.,Cohen, S.M.,Conti, E. Structural Insights Into the Notch-Modifying Glycosyltransferase Fringe Nat.Struct.Mol.Biol., 13:945-, 2006 Cited by PubMed Abstract: Fringe proteins are beta1,3-N-acetylglucosaminyltransferases that modify Notch receptors, altering their ligand-binding specificity to regulate Notch signaling in development. We present the crystal structure of mouse Manic Fringe bound to UDP and manganese. The structure reveals amino acid residues involved in recognition of donor substrates and catalysis, and a putative binding pocket for acceptor substrates. Mutations of several invariant residues in this pocket impair Fringe activity in vivo. PubMed: 16964258 DOI: 10.1038/NSMB1144 PDB entries with the same primary citation
Experimental method	X-RAY DIFFRACTION (2.1 Å)

Structure validation