1FOA

CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINYLTRANSFERASE I

Summary for 1FOA

• Entry DOI: 10.2210/pdb1foa/pdb
• Related: 1FO8 1FO9
• Descriptor: ALPHA-1,3-MANNOSYL-GLYCOPROTEIN BETA-1,2-N-ACETYLGLUCOSAMINYLTRANSFERASE, MANGANESE (II) ION, URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE, ... (5 entities in total)
• Functional Keywords: donor substrate and metal ion complex, alpha-1, 3-mannosyl-glycoprotein, beta-1, 2-n-acetylglucosaminyltransferase, n-acetylglucosaminyltransferase i, transferase
• Biological source: Oryctolagus cuniculus (rabbit)
• Cellular location: Golgi apparatus membrane; Single-pass type II membrane protein: P27115
• Total number of polymer chains: 1
• Total formula weight: 41299.48

Authors

Unligil, U.M.,Zhou, S.,Yuwaraj, S.,Sarkar, M.,Schachter, H.,Rini, J.M. (deposition date: 2000-08-26, release date: 2001-05-16, Last modification date: 2024-11-20)

Primary citation

Unligil, U.M.,Zhou, S.,Yuwaraj, S.,Sarkar, M.,Schachter, H.,Rini, J.M.
X-ray crystal structure of rabbit N-acetylglucosaminyltransferase I: catalytic mechanism and a new protein superfamily.
EMBO J., 19:5269-5280, 2000

PubMed Abstract: N:-acetylglucosaminyltransferase I (GnT I) serves as the gateway from oligomannose to hybrid and complex N:-glycans and plays a critical role in mammalian development and possibly all metazoans. We have determined the X-ray crystal structure of the catalytic fragment of GnT I in the absence and presence of bound UDP-GlcNAc/Mn(2+) at 1.5 and 1.8 A resolution, respectively. The structures identify residues critical for substrate binding and catalysis and provide evidence for similarity, at the mechanistic level, to the deglycosylation step of retaining beta-glycosidases. The structuring of a 13 residue loop, resulting from UDP-GlcNAc/Mn(2+) binding, provides an explanation for the ordered sequential 'Bi Bi' kinetics shown by GnT I. Analysis reveals a domain shared with Bacillus subtilis glycosyltransferase SpsA, bovine beta-1,4-galactosyl transferase 1 and Escherichia coli N:-acetylglucosamine-1-phosphate uridyltransferase. The low sequence identity, conserved fold and related functional features shown by this domain define a superfamily whose members probably share a common ancestor. Sequence analysis and protein threading show that the domain is represented in proteins from several glycosyltransferase families.

PubMed: 11032794
DOI: 10.1093/emboj/19.20.5269

Experimental method

X-RAY DIFFRACTION (1.8 Å)